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Volumn 584, Issue 12, 2010, Pages 2606-2617

A structural classification of substrate-binding proteins

Author keywords

ATP binding cassette transporter; Ligand receptor; Structural classification; Substrate binding protein; Tripartite ATP independent periplasmic transporter

Indexed keywords

ABC TRANSPORTER; ATRIAL NATRIURETIC FACTOR RECEPTOR; BINDING PROTEIN; IONOTROPIC RECEPTOR; METABOTROPIC RECEPTOR; SUBSTRATE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 77953127962     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.04.043     Document Type: Review
Times cited : (434)

References (61)
  • 2
    • 0015848303 scopus 로고
    • Different mechanisms of energy coupling for the active transport of proline and glutamine in Escherichia coli
    • Berger E.A. Different mechanisms of energy coupling for the active transport of proline and glutamine in Escherichia coli. Proc. Natl. Acad. Sci. USA 1973, 70:1514-1518.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 1514-1518
    • Berger, E.A.1
  • 3
    • 0016327218 scopus 로고
    • Different mechanisms of energy coupling for the shock-sensitive and shock-resistant amino acid permeases of Escherichia coli
    • Berger E.A., Heppel L.A. Different mechanisms of energy coupling for the shock-sensitive and shock-resistant amino acid permeases of Escherichia coli. J. Biol. Chem. 1974, 249:7747-7755.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7747-7755
    • Berger, E.A.1    Heppel, L.A.2
  • 4
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam R., Saier M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993, 57:320-346.
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier, M.H.2
  • 5
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes
    • Quiocho F.A., Ledvina P. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol. Microbiol. 1996, 20:17-25.
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.2
  • 6
    • 34047164005 scopus 로고    scopus 로고
    • Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding
    • Gonin S., Arnoux P., Pierru B., Lavergne J., Alonso B., Sabaty M., Pignol D. Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding. BMC Struct. Biol. 2007, 7:11.
    • (2007) BMC Struct. Biol. , vol.7 , pp. 11
    • Gonin, S.1    Arnoux, P.2    Pierru, B.3    Lavergne, J.4    Alonso, B.5    Sabaty, M.6    Pignol, D.7
  • 7
    • 60549098063 scopus 로고    scopus 로고
    • The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter
    • Mulligan C., Geertsma E., Severi E., Kelly D., Poolman B., Thomas G. The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter. Proc. Natl. Acad. Sci. USA 2009, 106:1778-1783.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1778-1783
    • Mulligan, C.1    Geertsma, E.2    Severi, E.3    Kelly, D.4    Poolman, B.5    Thomas, G.6
  • 9
    • 33544461370 scopus 로고    scopus 로고
    • The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors
    • Felder C.B., Graul R.C., Lee A.Y., Merkle H.P., Sadee W. The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. AAPS PharmSci. 1999, 1:1-20.
    • (1999) AAPS PharmSci. , vol.1 , pp. 1-20
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.P.4    Sadee, W.5
  • 10
    • 0036199366 scopus 로고    scopus 로고
    • Natriuretic peptide receptor: structure and signaling
    • Misono K.S. Natriuretic peptide receptor: structure and signaling. Mol. Cell Biochem. 2002, 230:49-60.
    • (2002) Mol. Cell Biochem. , vol.230 , pp. 49-60
    • Misono, K.S.1
  • 11
    • 0033636314 scopus 로고    scopus 로고
    • Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core
    • Armstrong N., Gouaux E. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 2000, 28:165-181.
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 13
    • 0029004903 scopus 로고
    • Crystal structure of lac repressor core tetramer and its implications for DNA looping
    • Friedman A.M., Fischmann T.O., Steitz T.A. Crystal structure of lac repressor core tetramer and its implications for DNA looping. Science 1995, 268:1721-1727.
    • (1995) Science , vol.268 , pp. 1721-1727
    • Friedman, A.M.1    Fischmann, T.O.2    Steitz, T.A.3
  • 14
    • 0028173030 scopus 로고
    • Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices
    • Schumacher M.A., Choi K.Y., Zalkin H., Brennan R.G. Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices. Science 1994, 266:763-770.
    • (1994) Science , vol.266 , pp. 763-770
    • Schumacher, M.A.1    Choi, K.Y.2    Zalkin, H.3    Brennan, R.G.4
  • 15
    • 0026621245 scopus 로고
    • ABC transporters: from microorganisms to man
    • Higgins C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 1992, 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 16
    • 31944431842 scopus 로고    scopus 로고
    • ABC transporter architecture and regulatory roles of accessory domains
    • Biemans-Oldehinkel E., Doeven M.K., Poolman B. ABC transporter architecture and regulatory roles of accessory domains. FEBS Lett. 2006, 580:1023-1035.
    • (2006) FEBS Lett. , vol.580 , pp. 1023-1035
    • Biemans-Oldehinkel, E.1    Doeven, M.K.2    Poolman, B.3
  • 17
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare D., Oldham M.L., Orelle C., Davidson A.L., Chen J. Alternating access in maltose transporter mediated by rigid-body rotations. Mol. Cell 2009, 33:528-536.
    • (2009) Mol. Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 18
    • 0036774002 scopus 로고    scopus 로고
    • ABC transporters: one, two or four extracytoplasmic substrate-binding sites?
    • van der Heide T., Poolman B. ABC transporters: one, two or four extracytoplasmic substrate-binding sites?. EMBO Rep. 2002, 3:938-943.
    • (2002) EMBO Rep. , vol.3 , pp. 938-943
    • van der Heide, T.1    Poolman, B.2
  • 19
    • 33644894229 scopus 로고    scopus 로고
    • Comparative and functional genomic analysis of prokaryotic nickel and cobalt uptake transporters: evidence for a novel group of ATP-binding cassette transporters
    • Rodionov D.A., Hebbeln P., Gelfand M.S., Eitinger T. Comparative and functional genomic analysis of prokaryotic nickel and cobalt uptake transporters: evidence for a novel group of ATP-binding cassette transporters. J. Bacteriol. 2006, 188:317-327.
    • (2006) J. Bacteriol. , vol.188 , pp. 317-327
    • Rodionov, D.A.1    Hebbeln, P.2    Gelfand, M.S.3    Eitinger, T.4
  • 22
    • 77950654738 scopus 로고    scopus 로고
    • Biochemical characterization of ThiT from Lactococcus lactis: a thiamin transporter with picomolar substrate binding affinity
    • Erkens G.B., Slotboom D.J. Biochemical characterization of ThiT from Lactococcus lactis: a thiamin transporter with picomolar substrate binding affinity. Biochemistry 2010, 49:3203-3212.
    • (2010) Biochemistry , vol.49 , pp. 3203-3212
    • Erkens, G.B.1    Slotboom, D.J.2
  • 23
    • 0034889137 scopus 로고    scopus 로고
    • The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea
    • Kelly D.J., Thomas G.H. The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea. FEMS Microbiol. Rev. 2001, 25:405-424.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 405-424
    • Kelly, D.J.1    Thomas, G.H.2
  • 24
    • 0030967906 scopus 로고    scopus 로고
    • TRAP transporters: a new family of periplasmic solute transport systems encoded by the dctPQM genes of Rhodobacter capsulatus and by homologs in diverse gram-negative bacteria
    • Forward J.A., Behrendt M.C., Wyborn N.R., Cross R., Kelly D.J. TRAP transporters: a new family of periplasmic solute transport systems encoded by the dctPQM genes of Rhodobacter capsulatus and by homologs in diverse gram-negative bacteria. J. Bacteriol. 1997, 179:5482-5493.
    • (1997) J. Bacteriol. , vol.179 , pp. 5482-5493
    • Forward, J.A.1    Behrendt, M.C.2    Wyborn, N.R.3    Cross, R.4    Kelly, D.J.5
  • 26
    • 0035794170 scopus 로고    scopus 로고
    • Guanylyl cyclase-linked natriuretic peptide receptors: structure and regulation
    • Potter L.R., Hunter T. Guanylyl cyclase-linked natriuretic peptide receptors: structure and regulation. J. Biol. Chem. 2001, 276:6057-6060.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6057-6060
    • Potter, L.R.1    Hunter, T.2
  • 27
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky A., Rosconi M., Gouaux E. X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 2009, 462:729-731.
    • (2009) Nature , vol.462 , pp. 729-731
    • Sobolevsky, A.1    Rosconi, M.2    Gouaux, E.3
  • 28
    • 4544356004 scopus 로고    scopus 로고
    • Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P
    • Schumacher M.A., Allen G.S., Diel M., Seidel G., Hillen W., Brennan R.G. Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P. Cell 2004, 118:731-741.
    • (2004) Cell , vol.118 , pp. 731-741
    • Schumacher, M.A.1    Allen, G.S.2    Diel, M.3    Seidel, G.4    Hillen, W.5    Brennan, R.G.6
  • 29
    • 0027444619 scopus 로고
    • In vitro binding of the pleiotropic transcriptional regulatory protein, FruR, to the fru, pps, ace, pts and icd operons of Escherichia coli and Salmonella typhimurium
    • Ramseier T.M., Nègre D., Cortay J.C., Scarabel M., Cozzone A.J., Saier M.H. In vitro binding of the pleiotropic transcriptional regulatory protein, FruR, to the fru, pps, ace, pts and icd operons of Escherichia coli and Salmonella typhimurium. J. Mol. Biol. 1993, 234:28-44.
    • (1993) J. Mol. Biol. , vol.234 , pp. 28-44
    • Ramseier, T.M.1    Nègre, D.2    Cortay, J.C.3    Scarabel, M.4    Cozzone, A.J.5    Saier, M.H.6
  • 30
    • 0016213770 scopus 로고
    • Crystallographic data of an l-arabinose-binding protein from Escherichia coli
    • Quiocho F.A., Phillips G.N., Spurlino J.C., Rodseth L.E. Crystallographic data of an l-arabinose-binding protein from Escherichia coli. J. Mol. Biol. 1974, 86:491-493.
    • (1974) J. Mol. Biol. , vol.86 , pp. 491-493
    • Quiocho, F.A.1    Phillips, G.N.2    Spurlino, J.C.3    Rodseth, L.E.4
  • 31
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    • Tang C., Schwieters C.D., Clore G.M. Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR. Nature 2007, 449:1078-1082.
    • (2007) Nature , vol.449 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, G.M.3
  • 32
    • 0020478556 scopus 로고
    • Hinge-bending in l-arabinose-binding protein. The Venus's-flytrap model
    • Mao B., Pear M., McCammon J., Quiocho F. Hinge-bending in l-arabinose-binding protein. The Venus's-flytrap model. J. Biol. Chem. 1982, 257:1131-1133.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1131-1133
    • Mao, B.1    Pear, M.2    McCammon, J.3    Quiocho, F.4
  • 33
    • 77749286394 scopus 로고    scopus 로고
    • Ligand-free open-closed transitions of periplasmic binding proteins: the case of glutamine-binding protein
    • Bermejo G.A., Strub M., Ho C., Tjandra N. Ligand-free open-closed transitions of periplasmic binding proteins: the case of glutamine-binding protein. Biochemistry 2010, 49:1893-1902.
    • (2010) Biochemistry , vol.49 , pp. 1893-1902
    • Bermejo, G.A.1    Strub, M.2    Ho, C.3    Tjandra, N.4
  • 34
    • 0037424465 scopus 로고    scopus 로고
    • Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding
    • Karpowich N.K., Huang H.H., Smith P.C., Hunt J.F. Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding. J. Biol. Chem. 2003, 278:8429-8434.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4
  • 35
    • 0036209769 scopus 로고    scopus 로고
    • The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation
    • Lee Y., Dorwart M.R., Hazlett K.R.O., Deka R.K., Norgard M.V., Radolf J.D., Hasemann C.A. The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation. J. Bacteriol. 2002, 184:2300-2304.
    • (2002) J. Bacteriol. , vol.184 , pp. 2300-2304
    • Lee, Y.1    Dorwart, M.R.2    Hazlett, K.R.O.3    Deka, R.K.4    Norgard, M.V.5    Radolf, J.D.6    Hasemann, C.A.7
  • 36
    • 17844398488 scopus 로고    scopus 로고
    • Ligand-free and -bound structures of the binding protein (LivJ) of the Escherichia coli ABC leucine/isoleucine/valine transport system: trajectory and dynamics of the interdomain rotation and ligand specificity
    • Trakhanov S., Vyas N., Luecke H., Kristensen D., Ma J., Quiocho F. Ligand-free and -bound structures of the binding protein (LivJ) of the Escherichia coli ABC leucine/isoleucine/valine transport system: trajectory and dynamics of the interdomain rotation and ligand specificity. Biochemistry 2005, 44:6597-6608.
    • (2005) Biochemistry , vol.44 , pp. 6597-6608
    • Trakhanov, S.1    Vyas, N.2    Luecke, H.3    Kristensen, D.4    Ma, J.5    Quiocho, F.6
  • 37
    • 0033548125 scopus 로고    scopus 로고
    • Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history
    • Fukami-Kobayashi K., Tateno Y., Nishikawa K. Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history. J. Mol. Biol. 1999, 286:279-290.
    • (1999) J. Mol. Biol. , vol.286 , pp. 279-290
    • Fukami-Kobayashi, K.1    Tateno, Y.2    Nishikawa, K.3
  • 38
    • 0024563996 scopus 로고
    • Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine
    • Sack J.S., Saper M.A., Quiocho F.A. Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine. J. Mol. Biol. 1989, 206:171-191.
    • (1989) J. Mol. Biol. , vol.206 , pp. 171-191
    • Sack, J.S.1    Saper, M.A.2    Quiocho, F.A.3
  • 39
    • 0024511371 scopus 로고
    • Structure of the l-leucine-binding protein refined at 2.4Å resolution and comparison with the Leu/Ile/Val-binding protein structure
    • Sack J.S., Trakhanov S.D., Tsigannik I.H., Quiocho F.A. Structure of the l-leucine-binding protein refined at 2.4Å resolution and comparison with the Leu/Ile/Val-binding protein structure. J. Mol. Biol. 1989, 206:193-207.
    • (1989) J. Mol. Biol. , vol.206 , pp. 193-207
    • Sack, J.S.1    Trakhanov, S.D.2    Tsigannik, I.H.3    Quiocho, F.A.4
  • 40
    • 0028067178 scopus 로고
    • The bacterial periplasmic histidine-binding protein. Structure/function analysis of the ligand-binding site and comparison with related proteins
    • Oh B.H., Kang C.H., Bondt H.D., Kim S.H., Nikaido K., Joshi A.K., Ames G.F. The bacterial periplasmic histidine-binding protein. Structure/function analysis of the ligand-binding site and comparison with related proteins. J. Biol. Chem. 1994, 269:4135-4143.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4135-4143
    • Oh, B.H.1    Kang, C.H.2    Bondt, H.D.3    Kim, S.H.4    Nikaido, K.5    Joshi, A.K.6    Ames, G.F.7
  • 42
    • 0032984288 scopus 로고    scopus 로고
    • Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
    • Lee Y.H., Deka R.K., Norgard M.V., Radolf J.D., Hasemann C.A. Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone. Nat. Struct. Biol. 1999, 6:628-633.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 628-633
    • Lee, Y.H.1    Deka, R.K.2    Norgard, M.V.3    Radolf, J.D.4    Hasemann, C.A.5
  • 45
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D: Biol. Crystallogr. 2004, 60:2256-2268.
    • (2004) Acta Crystallogr. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 46
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter binding protein complex BtuCD-BtuF
    • Hvorup R., Goetz B., Niederer M., Hollenstein K., Perozo E., Locher K. Asymmetry in the structure of the ABC transporter binding protein complex BtuCD-BtuF. Science 2007, 317:1387-1390.
    • (2007) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.1    Goetz, B.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.6
  • 47
    • 0037168666 scopus 로고    scopus 로고
    • The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter
    • Borths E.L., Locher K.P., Lee A.T., Rees D.C. The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Proc. Natl. Acad. Sci. USA 2002, 99:16642-16647.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16642-16647
    • Borths, E.L.1    Locher, K.P.2    Lee, A.T.3    Rees, D.C.4
  • 48
    • 10044241873 scopus 로고    scopus 로고
    • The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide
    • Levdikov V.M., Blagova E.V., Brannigan J.A., Wright L., Vagin A.A., Wilkinson A.J. The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide. J. Mol. Biol. 2005, 345:879-892.
    • (2005) J. Mol. Biol. , vol.345 , pp. 879-892
    • Levdikov, V.M.1    Blagova, E.V.2    Brannigan, J.A.3    Wright, L.4    Vagin, A.A.5    Wilkinson, A.J.6
  • 50
    • 0025754301 scopus 로고
    • The 2.3Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino J.C., Lu G.Y., Quiocho F.A. The 2.3Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 1991, 266:5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.Y.2    Quiocho, F.A.3
  • 51
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein K., Frei D.C., Locher K.P. Structure of an ABC transporter in complex with its binding protein. Nature 2007, 446:213-216.
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 55
    • 0020452292 scopus 로고
    • Associative properties of the Escherichia coli galactose binding protein and maltose binding protein
    • Richarme G. Associative properties of the Escherichia coli galactose binding protein and maltose binding protein. Biochem. Biophys. Res. Commun. 1982, 105:476-481.
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 476-481
    • Richarme, G.1
  • 56
    • 0021106975 scopus 로고
    • Associative properties of the Escherichia coli galactose-binding protein and maltose-binding protein
    • Richarme G. Associative properties of the Escherichia coli galactose-binding protein and maltose-binding protein. Biochim. Biophys. Acta 1983, 748:99-108.
    • (1983) Biochim. Biophys. Acta , vol.748 , pp. 99-108
    • Richarme, G.1
  • 57
    • 66149116873 scopus 로고    scopus 로고
    • Trapping open and closed forms of FitE: a group III periplasmic binding protein
    • Shi R., Proteau A., Wagner J., Cui Q., Purisima E.O., Matte A., Cygler M. Trapping open and closed forms of FitE: a group III periplasmic binding protein. Proteins 2009, 75:598-609.
    • (2009) Proteins , vol.75 , pp. 598-609
    • Shi, R.1    Proteau, A.2    Wagner, J.3    Cui, Q.4    Purisima, E.O.5    Matte, A.6    Cygler, M.7
  • 58
    • 33344456354 scopus 로고    scopus 로고
    • Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine
    • Horn C., Sohn-Bösser L., Breed J., Welte W., Schmitt L., Bremer E. Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine. J. Mol. Biol. 2006, 357:592-606.
    • (2006) J. Mol. Biol. , vol.357 , pp. 592-606
    • Horn, C.1    Sohn-Bösser, L.2    Breed, J.3    Welte, W.4    Schmitt, L.5    Bremer, E.6
  • 59
    • 49449086824 scopus 로고    scopus 로고
    • The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies
    • Smits S.H.J., Höing M., Lecher J., Jebbar M., Schmitt L., Bremer E. The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies. J. Bacteriol. 2008, 190:5663-5671.
    • (2008) J. Bacteriol. , vol.190 , pp. 5663-5671
    • Smits, S.H.J.1    Höing, M.2    Lecher, J.3    Jebbar, M.4    Schmitt, L.5    Bremer, E.6
  • 60
    • 9144257311 scopus 로고    scopus 로고
    • Structural basis for the binding of compatible solutes by ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus
    • Schiefner A., Holtmann G., Diederichs K., Welte W., Bremer E. Structural basis for the binding of compatible solutes by ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus. J. Biol. Chem. 2004, 279:48270-48281.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48270-48281
    • Schiefner, A.1    Holtmann, G.2    Diederichs, K.3    Welte, W.4    Bremer, E.5
  • 61
    • 34247210665 scopus 로고    scopus 로고
    • Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
    • Muto T., Tsuchiya D., Morikawa K., Jingami H. Structures of the extracellular regions of the group II/III metabotropic glutamate receptors. Proc. Natl. Acad. Sci. USA 2007, 104:3759-3764.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3759-3764
    • Muto, T.1    Tsuchiya, D.2    Morikawa, K.3    Jingami, H.4


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