메뉴 건너뛰기




Volumn 14, Issue 1, 2006, Pages 129-139

Crystal structure of human iron regulatory protein 1 as cytosolic aconitase

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; BACTERIAL ENZYME; IRON REGULATORY PROTEIN 1; MITOCHONDRIAL ENZYME;

EID: 33644804529     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.09.009     Document Type: Article
Times cited : (130)

References (51)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • J.P. Abrahams, and A.G.W. Leslie Methods used in the structure determination of bovine mitochondrial F1 ATPase Acta Crystallogr. D Biol. Crystallogr. 52 1996 30 42
    • (1996) Acta Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 2
    • 0030660482 scopus 로고    scopus 로고
    • Structure and dynamics of the iron responsive element RNA: Implications for binding of the RNA by iron regulatory binding proteins
    • K.J. Addess, J.P. Basilion, R.D. Klausner, T.A. Rouault, and A. Pardi Structure and dynamics of the iron responsive element RNA: implications for binding of the RNA by iron regulatory binding proteins J. Mol. Biol. 274 1997 72 83
    • (1997) J. Mol. Biol. , vol.274 , pp. 72-83
    • Addess, K.J.1    Basilion, J.P.2    Klausner, R.D.3    Rouault, T.A.4    Pardi, A.5
  • 3
    • 0028115810 scopus 로고
    • The iron-responsive element-binding protein: Localization of the RNA-binding site to the aconitase active-site cleft
    • J.P. Basilion, T.A. Rouault, C.M. Massinople, R.D. Klausner, and W.H. Burgess The iron-responsive element-binding protein: localization of the RNA-binding site to the aconitase active-site cleft Proc. Natl. Acad. Sci. USA 91 1994 574 578
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 574-578
    • Basilion, J.P.1    Rouault, T.A.2    Massinople, C.M.3    Klausner, R.D.4    Burgess, W.H.5
  • 4
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein
    • H. Beinert, M.C. Kennedy, and C.D. Stout Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein Chem. Rev. 96 1996 2335 2374
    • (1996) Chem. Rev. , vol.96 , pp. 2335-2374
    • Beinert, H.1    Kennedy, M.C.2    Stout, C.D.3
  • 5
    • 0037023698 scopus 로고    scopus 로고
    • Structural changes associated with switching activities of human iron regulatory protein 1
    • X. Brazzolotto, P. Timmins, Y. Dupont, and J.M. Moulis Structural changes associated with switching activities of human iron regulatory protein 1 J. Biol. Chem. 277 2002 11995 12000
    • (2002) J. Biol. Chem. , vol.277 , pp. 11995-12000
    • Brazzolotto, X.1    Timmins, P.2    Dupont, Y.3    Moulis, J.M.4
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 8
    • 13244277441 scopus 로고    scopus 로고
    • Aconitase couples metabolic regulation to mitochondrial DNA maintenance
    • X.J. Chen, X. Wang, B.A. Kaufman, and R.A. Butow Aconitase couples metabolic regulation to mitochondrial DNA maintenance Science 307 2005 714 717
    • (2005) Science , vol.307 , pp. 714-717
    • Chen, X.J.1    Wang, X.2    Kaufman, B.A.3    Butow, R.A.4
  • 9
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • S.S. Cooperman, E.G. Meyron-Holtz, H. Olivierre-Wilson, M.C. Ghosh, J.P. McConnell, and T.A. Rouault Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2 Blood 106 2005 1084 1091
    • (2005) Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1    Meyron-Holtz, E.G.2    Olivierre-Wilson, H.3    Ghosh, M.C.4    McConnell, J.P.5    Rouault, T.A.6
  • 10
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • E. de la Fortelle, and G. Bricogne Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods Methods Enzymol. 276 1997 472 494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 12
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • J.C. Drapier, H. Hirling, J. Wietzerbin, P. Kaldy, and L.C. Kuhn Biosynthesis of nitric oxide activates iron regulatory factor in macrophages EMBO J. 12 1993 3643 3649
    • (1993) EMBO J. , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kuhn, L.C.5
  • 15
    • 0141781072 scopus 로고    scopus 로고
    • A phosphomimetic mutation at Ser-138 renders iron regulatory protein 1 sensitive to iron-dependent degradation
    • C. Fillebeen, D. Chahine, A. Caltagirone, P. Segal, and K. Pantopoulos A phosphomimetic mutation at Ser-138 renders iron regulatory protein 1 sensitive to iron-dependent degradation Mol. Cell. Biol. 23 2003 6973 6981
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6973-6981
    • Fillebeen, C.1    Chahine, D.2    Caltagirone, A.3    Segal, P.4    Pantopoulos, K.5
  • 16
    • 19544363018 scopus 로고    scopus 로고
    • IRP1 Ser-711 is a phosphorylation site, critical for regulation of RNA-binding and aconitase activities
    • C. Fillebeen, A. Caltagirone, A. Martelli, J.M. Moulis, and K. Pantopoulos IRP1 Ser-711 is a phosphorylation site, critical for regulation of RNA-binding and aconitase activities Biochem. J. 388 2005 143 150
    • (2005) Biochem. J. , vol.388 , pp. 143-150
    • Fillebeen, C.1    Caltagirone, A.2    Martelli, A.3    Moulis, J.M.4    Pantopoulos, K.5
  • 17
    • 27144467097 scopus 로고    scopus 로고
    • Altered body iron distribution and microcytosis in mice deficient for Iron Regulatory Protein 2 (IRP2)
    • B. Galy, D. Ferring, B. Minana, O. Bell, H.G. Janser, M. Muckenthaler, K. Schumann, and M.W. Hentze Altered body iron distribution and microcytosis in mice deficient for Iron Regulatory Protein 2 (IRP2) Blood 106 2005 2580 2589
    • (2005) Blood , vol.106 , pp. 2580-2589
    • Galy, B.1    Ferring, D.2    Minana, B.3    Bell, O.4    Janser, H.G.5    Muckenthaler, M.6    Schumann, K.7    Hentze, M.W.8
  • 19
    • 0031033691 scopus 로고    scopus 로고
    • The aconitase family: Three structural variations on a common theme
    • M.J. Gruer, P.J. Artymiuk, and J.R. Guest The aconitase family: three structural variations on a common theme Trends Biochem. Sci. 22 1997 3 6
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 3-6
    • Gruer, M.J.1    Artymiuk, P.J.2    Guest, J.R.3
  • 20
    • 0029034338 scopus 로고
    • Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels
    • B. Guo, F.M. Brown, J.D. Phillips, Y. Yu, and E.A. Leibold Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels J. Biol. Chem. 270 1995 16529 16535
    • (1995) J. Biol. Chem. , vol.270 , pp. 16529-16535
    • Guo, B.1    Brown, F.M.2    Phillips, J.D.3    Yu, Y.4    Leibold, E.A.5
  • 21
    • 0027050315 scopus 로고
    • Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding
    • D.J. Haile, T.A. Rouault, J.B. Harford, M.C. Kennedy, G.A. Blondin, H. Beinert, and R.D. Klausner Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding Proc. Natl. Acad. Sci. USA 89 1992 11735 11739
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11735-11739
    • Haile, D.J.1    Rouault, T.A.2    Harford, J.B.3    Kennedy, M.C.4    Blondin, G.A.5    Beinert, H.6    Klausner, R.D.7
  • 22
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • M.W. Hentze, M.U. Muckenthaler, and N.C. Andrews Balancing acts: molecular control of mammalian iron metabolism Cell 117 2004 285 297
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 23
    • 0033230590 scopus 로고    scopus 로고
    • Identification of RNA-binding surfaces in iron regulatory protein-1
    • P. Kaldy, E. Menotti, R. Moret, and L.C. Kuhn Identification of RNA-binding surfaces in iron regulatory protein-1 EMBO J. 18 1999 6073 6083
    • (1999) EMBO J. , vol.18 , pp. 6073-6083
    • Kaldy, P.1    Menotti, E.2    Moret, R.3    Kuhn, L.C.4
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 27
    • 0029052367 scopus 로고
    • Steric and conformational features of the aconitase mechanism
    • H. Lauble, and C.D. Stout Steric and conformational features of the aconitase mechanism Proteins 22 1995 1 11
    • (1995) Proteins , vol.22 , pp. 1-11
    • Lauble, H.1    Stout, C.D.2
  • 28
    • 0026587755 scopus 로고
    • Crystal structures of aconitase with isocitrate and nitroisocitrate bound
    • H. Lauble, M.C. Kennedy, H. Beinert, and C.D. Stout Crystal structures of aconitase with isocitrate and nitroisocitrate bound Biochemistry 31 1992 2735 2748
    • (1992) Biochemistry , vol.31 , pp. 2735-2748
    • Lauble, H.1    Kennedy, M.C.2    Beinert, H.3    Stout, C.D.4
  • 29
    • 0034503620 scopus 로고    scopus 로고
    • CONSCRIPT: A program for generating electron density isosurfaces for presentation in protein crystallography
    • M.C. Lawrence, and P. Bourke CONSCRIPT: a program for generating electron density isosurfaces for presentation in protein crystallography J. Appl. Crystallogr. 33 2000 990 991
    • (2000) J. Appl. Crystallogr. , vol.33 , pp. 990-991
    • Lawrence, M.C.1    Bourke, P.2
  • 30
    • 0036614971 scopus 로고    scopus 로고
    • Cytosolic NADP(+)-dependent isocitrate dehydrogenase status modulates oxidative damage to cells
    • S.M. Lee, H.J. Koh, D.C. Park, B.J. Song, T.L. Huh, and J.W. Park Cytosolic NADP(+)-dependent isocitrate dehydrogenase status modulates oxidative damage to cells Free Radic. Biol. Med. 32 2002 1185 1196
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1185-1196
    • Lee, S.M.1    Koh, H.J.2    Park, D.C.3    Song, B.J.4    Huh, T.L.5    Park, J.W.6
  • 31
    • 0032100487 scopus 로고    scopus 로고
    • Analysis of ferritins in lymphoblastoid cell lines and in the lens of subjects with hereditary hyperferritinemia-cataract syndrome
    • S. Levi, D. Girelli, F. Perrone, M. Pasti, C. Beaumont, R. Corrocher, A. Albertini, and P. Arosio Analysis of ferritins in lymphoblastoid cell lines and in the lens of subjects with hereditary hyperferritinemia-cataract syndrome Blood 91 1998 4180 4187
    • (1998) Blood , vol.91 , pp. 4180-4187
    • Levi, S.1    Girelli, D.2    Perrone, F.3    Pasti, M.4    Beaumont, C.5    Corrocher, R.6    Albertini, A.7    Arosio, P.8
  • 32
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • R. Lill, and U. Muhlenhoff Iron-sulfur-protein biogenesis in eukaryotes Trends Biochem. Sci. 30 2005 133 141
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 133-141
    • Lill, R.1    Muhlenhoff, U.2
  • 33
    • 0033436322 scopus 로고    scopus 로고
    • The mechanism of aconitase: 1.8 Å resolution crystal structure of the S642a:citrate complex
    • S.J. Lloyd, H. Lauble, G.S. Prasad, and C.D. Stout The mechanism of aconitase: 1.8 Å resolution crystal structure of the S642a:citrate complex Protein Sci. 8 1999 2655 2662
    • (1999) Protein Sci. , vol.8 , pp. 2655-2662
    • Lloyd, S.J.1    Lauble, H.2    Prasad, G.S.3    Stout, C.D.4
  • 34
    • 0035805538 scopus 로고    scopus 로고
    • The hairpin loop but not the bulged C of the iron responsive element is essential for high affinity binding to iron regulatory protein-1
    • H.A. Meehan, and G.J. Connell The hairpin loop but not the bulged C of the iron responsive element is essential for high affinity binding to iron regulatory protein-1 J. Biol. Chem. 276 2001 14791 14796
    • (2001) J. Biol. Chem. , vol.276 , pp. 14791-14796
    • Meehan, H.A.1    Connell, G.J.2
  • 35
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 36
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • E.G. Meyron-Holtz, M.C. Ghosh, and T.A. Rouault Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo Science 306 2004 2087 2090
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 39
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: An update
    • K. Pantopoulos Iron metabolism and the IRE/IRP regulatory system: an update Ann. N Y Acad. Sci. 1012 2004 1 13
    • (2004) Ann. N Y Acad. Sci. , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 40
    • 0030942257 scopus 로고    scopus 로고
    • Differences in the regulation of iron regulatory protein-1 (IRP-1) by extra- and intracellular oxidative stress
    • K. Pantopoulos, S. Mueller, A. Atzberger, W. Ansorge, W. Stremmel, and M.W. Hentze Differences in the regulation of iron regulatory protein-1 (IRP-1) by extra- and intracellular oxidative stress J. Biol. Chem. 272 1997 9802 9808
    • (1997) J. Biol. Chem. , vol.272 , pp. 9802-9808
    • Pantopoulos, K.1    Mueller, S.2    Atzberger, A.3    Ansorge, W.4    Stremmel, W.5    Hentze, M.W.6
  • 41
    • 0030600134 scopus 로고    scopus 로고
    • Iron-sulphur clusters as genetic regulatory switches: The bifunctional iron regulatory protein-1
    • E. Paraskeva, and M.W. Hentze Iron-sulphur clusters as genetic regulatory switches: the bifunctional iron regulatory protein-1 FEBS Lett. 389 1996 40 43
    • (1996) FEBS Lett. , vol.389 , pp. 40-43
    • Paraskeva, E.1    Hentze, M.W.2
  • 42
    • 0028276577 scopus 로고
    • The bifunctional iron-responsive element binding protein/cytosolic aconitase: The role of active-site residues in ligand binding and regulation
    • C.C. Philpott, R.D. Klausner, and T.A. Rouault The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation Proc. Natl. Acad. Sci. USA 91 1994 7321 7325
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7321-7325
    • Philpott, C.C.1    Klausner, R.D.2    Rouault, T.A.3
  • 43
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • R.J. Read Pushing the boundaries of molecular replacement with maximum likelihood Acta Crystallogr. D Biol. Crystallogr. 57 2001 1373 1382
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 44
    • 0024383933 scopus 로고
    • The structure of aconitase
    • A.H. Robbins, and C.D. Stout The structure of aconitase Proteins 5 1989 289 312
    • (1989) Proteins , vol.5 , pp. 289-312
    • Robbins, A.H.1    Stout, C.D.2
  • 46
    • 0030842653 scopus 로고    scopus 로고
    • Probing the structure of the regulatory region of human transferrin receptor messenger RNA and its interaction with iron regulatory protein-1
    • J. Schlegl, V. Gegout, B. Schlager, M.W. Hentze, E. Westhof, C. Ehresmann, B. Ehresmann, and P. Romby Probing the structure of the regulatory region of human transferrin receptor messenger RNA and its interaction with iron regulatory protein-1 RNA 3 1997 1159 1172
    • (1997) RNA , vol.3 , pp. 1159-1172
    • Schlegl, J.1    Gegout, V.2    Schlager, B.3    Hentze, M.W.4    Westhof, E.5    Ehresmann, C.6    Ehresmann, B.7    Romby, P.8
  • 50
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • M.D. Winn, M.N. Isupov, and G.N. Murshudov Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallogr. D Biol. Crystallogr. 57 2001 122 133
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 51
    • 7444246744 scopus 로고    scopus 로고
    • Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme
    • Y. Yasutake, M. Yao, N. Sakai, T. Kirita, and I. Tanaka Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme J. Mol. Biol. 344 2004 325 333
    • (2004) J. Mol. Biol. , vol.344 , pp. 325-333
    • Yasutake, Y.1    Yao, M.2    Sakai, N.3    Kirita, T.4    Tanaka, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.