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Volumn 43, Issue 1, 2014, Pages 409-431

Metals in protein-protein interfaces

Author keywords

Interfacial metal clusters; Metal mediated oligomerization; Metal metallocofactors; Protein self assembly; Protein protein interactions

Indexed keywords

COPPER ION; METAL ION; METALLOPROTEIN; MULTIPROTEIN COMPLEX; NICKEL; TRANSITION ELEMENT; ZINC ION;

EID: 84901985721     PISSN: 1936122X     EISSN: 19361238     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-051013-023038     Document Type: Article
Times cited : (62)

References (101)
  • 1
    • 0032856157 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of the gamma-carbonic anhydrase from the methanoarchaeon Methanosarcina thermophila
    • Alber BE, Colangelo CM, Dong J, Stalhandske CMV, Baird TT, et al. 1999. Kinetic and spectroscopic characterization of the gamma-carbonic anhydrase from the methanoarchaeon Methanosarcina thermophila. Biochemistry 38:13119-288
    • (1999) Biochemistry , vol.38 , pp. 13119-13288
    • Alber, B.E.1    Colangelo, C.M.2    Dong, J.3    Stalhandske, C.M.V.4    Baird, T.T.5
  • 2
    • 57349112982 scopus 로고    scopus 로고
    • Elements and evolution
    • Anbar AD. 2008. Elements and evolution. Science 322:1481-833
    • (2008) Science , vol.322 , pp. 1481-1833
    • Anbar, A.D.1
  • 4
    • 84876571869 scopus 로고    scopus 로고
    • MetalPDB: A database of metal sites in biological macromolecular structures
    • Andreini C, Cavallaro G, Lorenzini S, Rosato A. 2013. MetalPDB: a database of metal sites in biological macromolecular structures. Nucleic Acids Res. 41:D312-199
    • (2013) Nucleic Acids Res. , vol.41
    • Andreini, C.1    Cavallaro, G.2    Lorenzini, S.3    Rosato, A.4
  • 5
    • 33744812407 scopus 로고    scopus 로고
    • Comparative genomics and structural biology of the molecular innovations of eukaryotes
    • Aravind L, Iyer LM, Koonin EV. 2006. Comparative genomics and structural biology of the molecular innovations of eukaryotes. Curr. Opin. Struct. Biol. 16:409-199
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 409-199
    • Aravind, L.1    Iyer, L.M.2    Koonin, E.V.3
  • 6
    • 0034649338 scopus 로고    scopus 로고
    • Mechanistic diversity in a metalloenzyme superfamily
    • Armstrong RN. 2000. Mechanistic diversity in a metalloenzyme superfamily. Biochemistry 39:13625-322
    • (2000) Biochemistry , vol.39 , pp. 13625-13332
    • Armstrong, R.N.1
  • 7
    • 31544482776 scopus 로고    scopus 로고
    • An architectural framework that may lie at the core of the postsynaptic density
    • Baron MK, Boeckers TM, Vaida B, Faham S, Gingery M, et al. 2006. An architectural framework that may lie at the core of the postsynaptic density. Science 311:531-355
    • (2006) Science , vol.311 , pp. 531-355
    • Baron, M.K.1    Boeckers, T.M.2    Vaida, B.3    Faham, S.4    Gingery, M.5
  • 8
    • 0022973592 scopus 로고
    • Ions binding to S100 proteins. I. Calcium-and zinc-binding properties of bovine brain S100α α, S100a (αβ), and S100b (β β) protein: Zn2+ regulates Ca2+ binding on S100b protein
    • Baudier J, Glasser N, Gerard D. 1986. Ions binding to S100 proteins. I. Calcium-and zinc-binding properties of bovine brain S100α α, S100a (αβ), and S100b (β β) protein: Zn2+ regulates Ca2+ binding on S100b protein. J. Biol. Chem. 261:8192-2033
    • (1986) J. Biol. Chem. , vol.261 , pp. 8192-2033
    • Baudier, J.1    Glasser, N.2    Gerard, D.3
  • 9
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett MJ, Schlunegger MP, Eisenberg D. 1995. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4:2455-688
    • (1995) Protein Sci. , vol.4 , pp. 2455-2688
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 10
    • 0032463747 scopus 로고    scopus 로고
    • All in the family: Structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly
    • Bergdoll M, Eltis LD, Cameron AD, Dumas P, Bolin JT. 1998. All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly. Protein Sci. 7:1661-700
    • (1998) Protein Sci. , vol.7 , pp. 1661-1700
    • Bergdoll, M.1    Eltis, L.D.2    Cameron, A.D.3    Dumas, P.4    Bolin, J.T.5
  • 14
    • 0032589790 scopus 로고    scopus 로고
    • Zn2+-binding and molecular determinants of tetramerization in voltage-gated K+ channels
    • Bixby KA, Nanao MH, Shen NV, Kreusch A, Bellamy H, et al. 1999. Zn2+-binding and molecular determinants of tetramerization in voltage-gated K+ channels. Nature 6:38-433
    • (1999) Nature , vol.6 , pp. 38-433
    • Bixby, K.A.1    Nanao, M.H.2    Shen, N.V.3    Kreusch, A.4    Bellamy, H.5
  • 15
    • 70350627430 scopus 로고    scopus 로고
    • Structural biology of copper trafficking
    • Boal AK, Rosenzweig AC. 2009. Structural biology of copper trafficking. Chem. Rev. 109:4760-799
    • (2009) Chem. Rev. , vol.109 , pp. 4760-4799
    • Boal, A.K.1    Rosenzweig, A.C.2
  • 17
    • 84860262383 scopus 로고    scopus 로고
    • Metal-directed, chemically tunable assembly of one-, two-and three-dimensional crystalline protein arrays
    • Brodin JD, Ambroggio XI, Tang C, Parent KN, Baker TS, Tezcan FA. 2012. Metal-directed, chemically tunable assembly of one-, two-and three-dimensional crystalline protein arrays. Nat. Chem. 4:375-822
    • (2012) Nat. Chem. , vol.4 , pp. 375-822
    • Brodin, J.D.1    Ambroggio, X.I.2    Tang, C.3    Parent, K.N.4    Baker, T.S.5    Tezcan, F.A.6
  • 19
    • 4644280162 scopus 로고    scopus 로고
    • ATP-driven electron transfer in enzymatic radical reactions
    • Buckel W, Hetzel M, Kim J. 2004. ATP-driven electron transfer in enzymatic radical reactions. Curr. Opin. Chem. Biol. 8:462-677
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 462-677
    • Buckel, W.1    Hetzel, M.2    Kim, J.3
  • 20
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess BK, Lowe DJ. 1996. Mechanism of molybdenum nitrogenase. Chem. Rev. 96:2983-30122
    • (1996) Chem. Rev. , vol.96 , pp. 2983-30122
    • Burgess, B.K.1    Lowe, D.J.2
  • 21
    • 0033550054 scopus 로고    scopus 로고
    • Reaction mechanism of glyoxalase i explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue
    • Cameron AD, Ridderstrm M, Olin B, Kavarana MJ, Creighton DJ, Mannervik B. 1999. Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue. Biochemistry 38:13480-900
    • (1999) Biochemistry , vol.38 , pp. 13480-13900
    • Cameron, A.D.1    Ridderstrm, M.2    Olin, B.3    Kavarana, M.J.4    Creighton, D.J.5    Mannervik, B.6
  • 22
    • 0043192605 scopus 로고    scopus 로고
    • Molecular basis ofmetal-ion selectivity and zeptomolar sensitivity by CueR
    • Changela A, Chen K, Xue Y,Holschen J,Outten CE, et al. 2003. Molecular basis ofmetal-ion selectivity and zeptomolar sensitivity by CueR. Science 301:1383-877
    • (2003) Science , vol.301 , pp. 1383-1877
    • Changela, A.1    Chen, K.2    Xue, Y.3    Holschen, J.4    Outten, C.E.5
  • 23
    • 2342429689 scopus 로고    scopus 로고
    • Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP
    • Chao Y, Fu D. 2004. Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP. J. Biol. Chem. 279:17173-800
    • (2004) J. Biol. Chem. , vol.279 , pp. 17173-17800
    • Chao, Y.1    Fu, D.2
  • 25
    • 0000726701 scopus 로고    scopus 로고
    • Carbonic anhydrase: Evolution of the zinc binding site by nature and by design
    • Christianson DW, Fierke CA. 1996. Carbonic anhydrase: evolution of the zinc binding site by nature and by design. Acc. Chem. Res. 29:331-399
    • (1996) Acc. Chem. Res. , vol.29 , pp. 331-399
    • Christianson, D.W.1    Fierke, C.A.2
  • 26
    • 0028266674 scopus 로고
    • Crystallographic evidence for dual coordination around zinc in the T3R3 human insulin hexamer
    • Ciszak E, Smith GD. 1994. Crystallographic evidence for dual coordination around zinc in the T3R3 human insulin hexamer. Biochemistry 33:1512-177
    • (1994) Biochemistry , vol.33 , pp. 1512-1187
    • Ciszak, E.1    Smith, G.D.2
  • 27
    • 0042065267 scopus 로고    scopus 로고
    • Characterization of the roles of NikR, a nickel-responsive pleiotropic autoregulator of Helicobacter pylori
    • ContrerasM, Thiberge J-M,Mandrand-BerthelotM-A, Labigne A. 2003. Characterization of the roles of NikR, a nickel-responsive pleiotropic autoregulator of Helicobacter pylori. Mol. Microbiol. 49:947-633
    • (2003) Mol. Microbiol. , vol.49 , pp. 947-633
    • Contreras, M.1    Thiberge, J.-M.2    Mandrand-Berthelot, M.-A.3    Labigne, A.4
  • 28
    • 84873440467 scopus 로고    scopus 로고
    • Inward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopy
    • Coudray N, Valvo S, Hu M, Lasala R, Kim C, et al. 2013. Inward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopy. Proc. Natl. Acad. Sci. USA 110:2140-455
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 2140-2455
    • Coudray, N.1    Valvo, S.2    Hu, M.3    Lasala, R.4    Kim, C.5
  • 29
    • 0028618538 scopus 로고
    • Supramolecular self-assembly of glutamine synthetase: Mutagenesis of a novel intermolecular metal binding site required for dodecamer stacking
    • DabrowskiMJ, Yanchunas J, Villafranca BC, Dietze EC, Schurke P, Atkins WM. 1994. Supramolecular self-assembly of glutamine synthetase: mutagenesis of a novel intermolecular metal binding site required for dodecamer stacking. Biochemistry 33:14957-644
    • (1994) Biochemistry , vol.33 , pp. 14957-14654
    • Dabrowski, M.J.1    Yanchunas, J.2    Villafranca, B.C.3    Dietze, E.C.4    Schurke, P.5    Atkins, W.M.6
  • 30
    • 84860773275 scopus 로고    scopus 로고
    • Catalysis by a de novo zinc-mediated protein interface: Implications for natural enzyme evolution and rational enzyme engineering
    • Der BS, Edwards DR, Kuhlman B. 2012. Catalysis by a de novo zinc-mediated protein interface: implications for natural enzyme evolution and rational enzyme engineering. Biochemistry 51:3933-400
    • (2012) Biochemistry , vol.51 , pp. 3933-3410
    • Der Edwards, B.S.D.R.1    Kuhlman, B.2
  • 31
    • 33746849786 scopus 로고    scopus 로고
    • Structural basis of the nickel response in Helicobacter pylori: Crystal structures of HpNikR in apo and nickel-bound states
    • Dian C, Schauer K, Kapp U, McSweeney SM, Labigne A, Terradot L. 2006. Structural basis of the nickel response in Helicobacter pylori: crystal structures of HpNikR in apo and nickel-bound states. J. Mol. Biol. 361:715-300
    • (2006) J. Mol. Biol. , vol.361 , pp. 715-300
    • Dian, C.1    Schauer, K.2    Kapp, U.3    McSweeney, S.M.4    Labigne, A.5    Terradot, L.6
  • 32
    • 0035902973 scopus 로고    scopus 로고
    • Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster
    • DobbekH, Svetlitchnyi V, Gremer L,Huber R,Meyer O. 2001. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science 293:1281-855
    • (2001) Science , vol.293 , pp. 1281-1855
    • Dobbek, H.1    Svetlitchnyi, V.2    Gremer, L.3    Huber, R.4    Meyer, O.5
  • 33
    • 68949209635 scopus 로고    scopus 로고
    • Dicamba monooxygenase: Structural insights into a dynamic Rieske oxygenase that catalyzes an exocyclic monooxygenation
    • D'Ordine RL, Rydel TJ, Storek MJ, Sturman EJ, Moshiri F, et al. 2009. Dicamba monooxygenase: structural insights into a dynamic Rieske oxygenase that catalyzes an exocyclic monooxygenation. J. Mol. Biol. 392:481-977
    • (2009) J. Mol. Biol. , vol.392 , pp. 481-977
    • D'Ordine, R.L.1    Rydel, T.J.2    Storek, M.J.3    Sturman, E.J.4    Moshiri, F.5
  • 34
    • 0035834117 scopus 로고    scopus 로고
    • Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase
    • Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW. 2001. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc. Natl. Acad. Sci. USA 98:11973-788
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11973-11798
    • Drennan, C.L.1    Heo, J.2    Sintchak, M.D.3    Schreiter, E.4    Ludden, P.W.5
  • 35
    • 24744439439 scopus 로고    scopus 로고
    • Zinc-ligand interactions modulate assembly and stability of the insulin hexamer - A review
    • Dunn MF. 2005. Zinc-ligand interactions modulate assembly and stability of the insulin hexamer - A review. Biometals 18:295-3033
    • (2005) Biometals , vol.18 , pp. 295-3033
    • Dunn, M.F.1
  • 38
    • 78049277867 scopus 로고    scopus 로고
    • Natural and amyloid self-assembly of S100 proteins: Structural basis of functional diversity
    • Fritz G, Botelho HM, Morozova-Roche LA, Gomes CM. 2010. Natural and amyloid self-assembly of S100 proteins: structural basis of functional diversity. FEBS J. 277:4578-900
    • (2010) FEBS J. , vol.277 , pp. 4578-4900
    • Fritz, G.1    Botelho, H.M.2    Morozova-Roche, L.A.3    Gomes, C.M.4
  • 39
    • 0017663070 scopus 로고
    • Zinc ion-induced assembly of tubulin
    • Gaskin F, Kress Y. 1977. Zinc ion-induced assembly of tubulin. J. Biol. Chem. 252:6918-244
    • (1977) J. Biol. Chem. , vol.252 , pp. 6918-6254
    • Gaskin, F.1    Kress, Y.2
  • 41
    • 0034029015 scopus 로고    scopus 로고
    • Aromatic hydrocarbon dioxygenases in environmental biotechnology
    • Gibson DT, Parales RE. 2000. Aromatic hydrocarbon dioxygenases in environmental biotechnology. Curr. Opin. Biotechnol. 11:236-433
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 236-433
    • Gibson, D.T.1    Parales, R.E.2
  • 42
    • 84859466163 scopus 로고    scopus 로고
    • Redox-dependent complex formation by an ATPdependent activator of the corrinoid/iron-sulfur protein
    • Hennig SE, Jeoung J-H, Goetzl S, Dobbek H. 2012. Redox-dependent complex formation by an ATPdependent activator of the corrinoid/iron-sulfur protein. Proc. Natl. Acad. Sci. USA 109:5235-400
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5235-5400
    • Hennig, S.E.1    Jeoung, J.-H.2    Goetzl, S.3    Dobbek, H.4
  • 43
    • 0036682314 scopus 로고    scopus 로고
    • The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair
    • Hopfner KP, Craig L, Moncalian G, Zinkel RA, Usui T, et al. 2002. The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair. Nature 418:562-666
    • (2002) Nature , vol.418 , pp. 562-666
    • Hopfner, K.P.1    Craig, L.2    Moncalian, G.3    Zinkel, R.A.4    Usui, T.5
  • 44
    • 7744224797 scopus 로고    scopus 로고
    • Structural basis of biological nitrogen fixation
    • Howard JB, Rees DC. 1996. Structural basis of biological nitrogen fixation. Chem. Rev. 96:2965-822
    • (1996) Chem. Rev. , vol.96 , pp. 2965-2832
    • Howard, J.B.1    Rees, D.C.2
  • 46
    • 0034622579 scopus 로고    scopus 로고
    • A closer look at the active site of gammaclass carbonic anhydrases: High-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila
    • Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC. 2000. A closer look at the active site of gammaclass carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry 39:9222-311
    • (2000) Biochemistry , vol.39 , pp. 9222-9311
    • Iverson, T.M.1    Alber, B.E.2    Kisker, C.3    Ferry, J.G.4    Rees, D.C.5
  • 49
    • 0034721678 scopus 로고    scopus 로고
    • Signal-processing machines at the postsynaptic density
    • Kennedy MB. 2000. Signal-processing machines at the postsynaptic density. Science 290:750-544
    • (2000) Science , vol.290 , pp. 750-544
    • Kennedy, M.B.1
  • 50
    • 0141654999 scopus 로고    scopus 로고
    • A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8
    • Kim PW, Sun Z-YJ, Blacklow SC, Wagner G, Eck MJ. 2003. A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8. Science 301:1725-288
    • (2003) Science , vol.301 , pp. 1725-1298
    • Kim, P.W.1    Z-Yj, S.2    Blacklow, S.C.3    Wagner, G.4    Eck, M.J.5
  • 51
    • 78149336385 scopus 로고    scopus 로고
    • Zinc binding drives sheet formation by the SAM domain of diacylglycerol kinase?
    • Knight MJ, Joubert MK, Plotkowski ML, Kropat J, Gingery M, et al. 2010. Zinc binding drives sheet formation by the SAM domain of diacylglycerol kinase. Biochemistry 49:9667-766
    • (2010) Biochemistry , vol.49 , pp. 9667-9766
    • Knight, M.J.1    Joubert, M.K.2    Plotkowski, M.L.3    Kropat, J.4    Gingery, M.5
  • 52
    • 33847298449 scopus 로고    scopus 로고
    • Crystal structure of CO-sensing transcription activator CooA bound to exogenous ligand imidazole
    • Komori H, Inagaki S,Yoshioka S,Aono S,Higuchi Y. 2007. Crystal structure of CO-sensing transcription activator CooA bound to exogenous ligand imidazole. J. Mol. Biol. 367:864-711
    • (2007) J. Mol. Biol. , vol.367 , pp. 864-711
    • Komori, H.1    Inagaki, S.2    Yoshioka, S.3    Aono, S.4    Higuchi, Y.5
  • 53
    • 0035191642 scopus 로고    scopus 로고
    • Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil
    • Krantz BA, Sosnick TR. 2001. Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil. Nat. Struct. Biol. 8:1042-477
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1042-1477
    • Krantz, B.A.1    Sosnick, T.R.2
  • 54
    • 34548232365 scopus 로고    scopus 로고
    • Inference ofmacromolecular assemblies from crystalline state
    • Krissinel E,Henrick K. 2007. Inference ofmacromolecular assemblies from crystalline state. J. Mol. Biol. 372:774-977
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-977
    • Krissinel, E.1    Henrick, K.2
  • 56
    • 0035253047 scopus 로고    scopus 로고
    • Zinc finger proteins: New insights into structural and functional diversity
    • Laity JH, Lee BM, Wright PE. 2001. Zinc finger proteins: new insights into structural and functional diversity. Curr. Opin. Struct. Biol. 11:39-466
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 39-466
    • Laity, J.H.1    Lee, B.M.2    Wright, P.E.3
  • 57
    • 25444494469 scopus 로고    scopus 로고
    • The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale
    • Lepore BW, Ruzicka FJ, Frey PA, Ringe D. 2005. The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale. Proc. Natl. Acad. Sci. USA 102:13819-244
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13819-13254
    • Lepore, B.W.1    Ruzicka, F.J.2    Frey, P.A.3    Ringe, D.4
  • 58
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of αβ-tubulin at 3.5 Å resolution
    • Löwe J, Li H, Downing KH, Nogales E. 2001. Refined structure of αβ-tubulin at 3.5 Å resolution. J. Mol. Biol. 313:1045-577
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1577
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 59
    • 70349789244 scopus 로고    scopus 로고
    • Structural basis for autoregulation of the zinc transporter YiiP
    • Lu M, Chai J, Fu D. 2009. Structural basis for autoregulation of the zinc transporter YiiP. Nat. Struct. Mol. Biol. 16:1063-677
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1063-1677
    • Lu, M.1    Chai, J.2    Fu, D.3
  • 60
    • 70349272618 scopus 로고    scopus 로고
    • The structural basis of tail-anchored membrane protein recognition by Get3
    • Mateja A, Szlachcic A, Downing ME, Dobosz M, Mariappan M, et al. 2009. The structural basis of tail-anchored membrane protein recognition by Get3. Nature 461:361-666
    • (2009) Nature , vol.461 , pp. 361-666
    • Mateja, A.1    Szlachcic, A.2    Downing, M.E.3    Dobosz, M.4    Mariappan, M.5
  • 61
    • 80051944480 scopus 로고    scopus 로고
    • A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein
    • Matoba Y, Bando N, Oda K, Noda M, Higashikawa F, et al. 2011. A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein. J. Biol. Chem. 286:30219-311
    • (2011) J. Biol. Chem. , vol.286 , pp. 30219-30311
    • Matoba, Y.1    Bando, N.2    Oda, K.3    Noda, M.4    Higashikawa, F.5
  • 62
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M. 2006. Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 281:8981-900
    • (2006) J. Biol. Chem. , vol.281 , pp. 8981-8910
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 63
    • 84882257567 scopus 로고    scopus 로고
    • In vitro and cellular self-assembly of a Zn-binding protein cryptand via templated disulfide bonds
    • Medina-Morales A, Perez A, Brodin JD, Tezcan FA. 2013. In vitro and cellular self-assembly of a Zn-binding protein cryptand via templated disulfide bonds. J. Am. Chem. Soc. 135:12013-222
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12013-12222
    • Medina-Morales, A.1    Perez, A.2    Brodin, J.D.3    Tezcan, F.A.4
  • 64
    • 77956926334 scopus 로고    scopus 로고
    • Structural characterization of a microperoxidase inside a metal-directed protein cage
    • Ni TW, Tezcan FA. 2010. Structural characterization of a microperoxidase inside a metal-directed protein cage. Angew. Chem. Int. Ed. 49:7014-188
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 7014-7188
    • Ni, T.W.1    Tezcan, F.A.2
  • 65
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales E,Wolf SG, Downing KH. 1998. Structure of the αβ tubulin dimer by electron crystallography. Nature 391:199-2033
    • (1998) Nature , vol.391 , pp. 199-2033
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 66
    • 67650540770 scopus 로고    scopus 로고
    • Identification of the Zn2+ binding site and mode of operation of a mammalian Zn2+ transporter
    • Ohana E, Hoch E, Keasar C, Kambe T, Yifrach O, et al. 2009. Identification of the Zn2+ binding site and mode of operation of a mammalian Zn2+ transporter. J. Biol. Chem. 284:17677-866
    • (2009) J. Biol. Chem. , vol.284 , pp. 17677-17866
    • Ohana, E.1    Hoch, E.2    Keasar, C.3    Kambe, T.4    Yifrach, O.5
  • 67
    • 79955645914 scopus 로고    scopus 로고
    • The crystal structures of human S100B in the zinc-and calcium-loaded state at three pH values reveal zinc ligand swapping
    • Ostendorp T, Diez J, Heizmann CW, Fritz G. 2011. The crystal structures of human S100B in the zinc-and calcium-loaded state at three pH values reveal zinc ligand swapping. Biochim. Biophys. Acta 1813:1083-911
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1083-1911
    • Ostendorp, T.1    Diez, J.2    Heizmann, C.W.3    Fritz, G.4
  • 68
    • 7944231534 scopus 로고    scopus 로고
    • Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation
    • Palacios EH, Weiss A. 2004. Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation. Oncogene 23:7990-80000
    • (2004) Oncogene , vol.23 , pp. 7990-80000
    • Palacios, E.H.1    Weiss, A.2
  • 69
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom resolution
    • Peters JW,LanzilottaWN,Lemon BJ, Seefeldt LC. 1998. X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom resolution. Science 282:1853-588
    • (1998) Science , vol.282 , pp. 1853-1598
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 70
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello PJ, Demple B. 2001. Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol. 19:109-144
    • (2001) Trends Biotechnol. , vol.19 , pp. 109-144
    • Pomposiello, P.J.1    Demple, B.2
  • 71
    • 44849102395 scopus 로고    scopus 로고
    • Metals in neurobiology: Probing their chemistry and biology with molecular imaging
    • Que EL, Domaille DW, Chang CJ. 2008. Metals in neurobiology: probing their chemistry and biology with molecular imaging. Chem. Rev. 108:1517-499
    • (2008) Chem. Rev. , vol.108 , pp. 1517-1499
    • Que, E.L.1    Domaille, D.W.2    Chang, C.J.3
  • 72
    • 35548991935 scopus 로고    scopus 로고
    • Deducing the energetic cost of protein folding in zinc finger proteins using designed metallopeptides
    • Reddi AR, Guzman TR, Breece RM, Tiemey DL, Gibney BR. 2007. Deducing the energetic cost of protein folding in zinc finger proteins using designed metallopeptides. J. Am. Chem. Soc. 129:12815-277
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12815-12287
    • Reddi, A.R.1    Guzman, T.R.2    Breece, R.M.3    Tiemey, D.L.4    Gibney, B.R.5
  • 73
  • 74
    • 33748939410 scopus 로고    scopus 로고
    • Early protein evolution: Building domains from ligand-binding polypeptide segments
    • Riechmann L,WinterG. 2006. Early protein evolution: building domains from ligand-binding polypeptide segments. J. Mol. Biol. 363:460-688
    • (2006) J. Mol. Biol. , vol.363 , pp. 460-688
    • Riechmann, L.1    Winter, G.2
  • 75
    • 33846016897 scopus 로고    scopus 로고
    • Crystal structure analysis and solution studies of human Lck-SH3; Zinc-induced homodimerization competes with the binding of proline-rich motifs
    • Romir J, Lilie H, Egerer-Sieber C, Bauer F, Sticht H, Muller YA. 2007. Crystal structure analysis and solution studies of human Lck-SH3; zinc-induced homodimerization competes with the binding of proline-rich motifs. J. Mol. Biol. 365:1417-288
    • (2007) J. Mol. Biol. , vol.365 , pp. 1417-1298
    • Romir, J.1    Lilie, H.2    Egerer-Sieber, C.3    Bauer, F.4    Sticht, H.5    Muller, Y.A.6
  • 76
    • 0042232277 scopus 로고    scopus 로고
    • Alanine-scanning mutations in domain 4 of anthrax toxin protective antigen reveal residues important for binding to the cellular receptor and to a neutralizing monoclonal antibody
    • Rosovitz MJ, Schuck P, Varughese M, Chopra AP, Mehra V, et al. 2003. Alanine-scanning mutations in domain 4 of anthrax toxin protective antigen reveal residues important for binding to the cellular receptor and to a neutralizing monoclonal antibody. J. Biol. Chem. 278:30936-444
    • (2003) J. Biol. Chem. , vol.278 , pp. 30936-30454
    • Rosovitz, M.J.1    Schuck, P.2    Varughese, M.3    Chopra, A.P.4    Mehra, V.5
  • 77
    • 17044378032 scopus 로고    scopus 로고
    • Shank expression is sufficient to induce functional dendritic spine synapses in aspiny neurons
    • Roussignol G, Ango F, Romorini S, Tu JC, Sala C, et al. 2005. Shank expression is sufficient to induce functional dendritic spine synapses in aspiny neurons. J. Neurosci. 25:3560-700
    • (2005) J. Neurosci. , vol.25 , pp. 3560-3700
    • Roussignol, G.1    Ango, F.2    Romorini, S.3    Tu, J.C.4    Sala, C.5
  • 79
    • 64349084476 scopus 로고    scopus 로고
    • Control of protein oligomerization symmetry bymetal coordination:C2 andC3 symmetrical assemblies through CuII andNiII coordination
    • Salgado EN, Lewis RA, Mossin S, Rheingold AL, Tezcan FA. 2009. Control of protein oligomerization symmetry bymetal coordination:C2 andC3 symmetrical assemblies through CuII andNiII coordination. Inorg. Chem. 48:2726-288
    • (2009) Inorg. Chem. , vol.48 , pp. 2726-2298
    • Salgado, E.N.1    Lewis, R.A.2    Mossin, S.3    Rheingold, A.L.4    Tezcan, F.A.5
  • 80
    • 3542993051 scopus 로고    scopus 로고
    • Crystal structure of a complex between anthrax toxin and its host cell receptor
    • Santelli E, Bankston LA, Leppla SH, Liddington RC. 2004. Crystal structure of a complex between anthrax toxin and its host cell receptor. Nature 430:905-88
    • (2004) Nature , vol.430 , pp. 905-988
    • Santelli, E.1    Bankston, L.A.2    Leppla, S.H.3    Liddington, R.C.4
  • 81
    • 0030611701 scopus 로고    scopus 로고
    • Structure of ADP·IF4-stabilized nitrogenase complex and its implications for signal transduction
    • Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC. 1997. Structure of ADP·IF4-stabilized nitrogenase complex and its implications for signal transduction. Nature 387:370-766
    • (1997) Nature , vol.387 , pp. 370-766
    • Schindelin, H.1    Kisker, C.2    Schlessman, J.L.3    Howard, J.B.4    Rees, D.C.5
  • 82
    • 33748773334 scopus 로고    scopus 로고
    • NikR-operator complex structure and the mechanism of repressor activation by metal ions
    • Schreiter ER, Wang SC, Zamble DB, Drennan CL. 2006. NikR-operator complex structure and the mechanism of repressor activation by metal ions. Proc. Natl. Acad. Sci. USA 103:13676-811
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13676-13811
    • Schreiter, E.R.1    Wang, S.C.2    Zamble, D.B.3    Drennan, C.L.4
  • 83
    • 0030856066 scopus 로고    scopus 로고
    • CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein
    • Shelver D, Kerby RL, He Y, Roberts GP. 1997. CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein. Proc. Natl. Acad. Sci. USA 94:11216-200
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11216-11210
    • Shelver, D.1    Kerby, R.L.2    He, Y.3    Roberts, G.P.4
  • 86
    • 80051474125 scopus 로고    scopus 로고
    • Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex
    • Stefer S, Reitz S,Wang F,Wild K, Pang Y-Y, et al. 2011. Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex. Science 333:758-622
    • (2011) Science , vol.333 , pp. 758-622
    • Stefer, S.1    Reitz, S.2    Wang, F.3    Wild, K.4    Pang, Y.-Y.5
  • 87
    • 84956971564 scopus 로고    scopus 로고
    • The role of metal ions in neurology. An introduction
    • ed. A Sigel, H Sigel, RKO Sigel, Chichester, UK: Wileyy
    • Strozyk D, Bush AI. 2006. The role of metal ions in neurology. An introduction. In Neurodegenerative Diseases and Metal Ions, ed. A Sigel, H Sigel, RKO Sigel, pp. 1:1-7. Chichester, UK:Wileyy
    • (2006) Neurodegenerative Diseases and Metal Ions , pp. 1-7
    • Strozyk, D.1    Bush, A.I.2
  • 88
    • 38849143765 scopus 로고    scopus 로고
    • Carbonic anhydrases: Novel therapeutic applications for inhibitors and activators
    • Supuran CT. 2008. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat. Rev. Drug Discov. 7:168-811
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 168-811
    • Supuran, C.T.1
  • 90
    • 0025298551 scopus 로고
    • The glyoxalase system: New developments towards functional characterization of a metabolic pathway fundamental to biological life
    • Thornalley PJ. 1990. The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269:1-111
    • (1990) Biochem. J. , vol.269 , pp. 1-111
    • Thornalley, P.J.1
  • 91
    • 0024961847 scopus 로고
    • Pseudo 2-fold symmetry in the copper-binding domain of arthropodan haemocyanins: Possible implications for the evolution of oxygen transport proteins
    • Volbeda A, Hol WGJ. 1989. Pseudo 2-fold symmetry in the copper-binding domain of arthropodan haemocyanins: possible implications for the evolution of oxygen transport proteins. J. Mol. Biol. 206:531-466
    • (1989) J. Mol. Biol. , vol.206 , pp. 531-466
    • Volbeda, A.1    Hol, W.G.J.2
  • 93
    • 41949137280 scopus 로고    scopus 로고
    • Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA
    • Watanabe S, Kita A, Kobayashi K,Miki K. 2008. Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA. Proc. Natl. Acad. Sci. USA 105:4121-266
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4121-4266
    • Watanabe, S.1    Kita, A.2    Kobayashi, K.3    Miki, K.4
  • 94
    • 33747706168 scopus 로고    scopus 로고
    • Binding and transport ofmetal ions at the dimer interface of the Escherichia coli metal transporter YiiP
    • Wei Y, FuD. 2006. Binding and transport ofmetal ions at the dimer interface of the Escherichia coli metal transporter YiiP. J. Biol. Chem. 281:23492-5022
    • (2006) J. Biol. Chem. , vol.281 , pp. 23492-25022
    • Wei, Y.1    Fu, D.2
  • 95
    • 84866540561 scopus 로고    scopus 로고
    • Dynamic structural changes are observed upon collagen and metal ion binding to the integrin α1 i domain
    • Weinreb PH, Li S, Gao SX, Liu T, Pepinsky RB, et al. 2012. Dynamic structural changes are observed upon collagen and metal ion binding to the integrin α1 I domain. J. Biol. Chem. 287:32897-9122
    • (2012) J. Biol. Chem. , vol.287 , pp. 32897-39122
    • Weinreb, P.H.1    Li, S.2    Gao, S.X.3    Liu, T.4    Pepinsky, R.B.5
  • 97
    • 84859583743 scopus 로고    scopus 로고
    • Ni(II) coordination to mixed sites modulates DNA binding of HpNikR via a long-range effect
    • West AL, Evans SE, Gonzlez JM, Carter LG, Tsuruta H, et al. 2012. Ni(II) coordination to mixed sites modulates DNA binding of HpNikR via a long-range effect. Proc. Natl. Acad. Sci. USA 109:5633-388
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5633-5398
    • West, A.L.1    Evans, S.E.2    Gonzlez, J.M.3    Carter, L.G.4    Tsuruta, H.5
  • 99
    • 1342346631 scopus 로고    scopus 로고
    • Functionally critical elements of CooA-related CO sensors
    • Youn H, Kerby RL, Conrad M, Roberts GP. 2004. Functionally critical elements of CooA-related CO sensors. J. Bacteriol. 186:1320-299
    • (2004) J. Bacteriol. , vol.186 , pp. 1320-1299
    • Youn, H.1    Kerby, R.L.2    Conrad, M.3    Roberts, G.P.4
  • 101


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