메뉴 건너뛰기




Volumn 22, Issue 3, 2014, Pages 431-443

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE PROTEIN; DISULFIDE; ENDOPLASMIC RETICULUM P46 PROTEIN; PEROXIREDOXIN 4; PROTEIN DISULFIDE ISOMERASE; THIOREDOXIN; UNCLASSIFIED DRUG; APROTININ; OXYGEN; TXNDC5 PROTEIN, HUMAN;

EID: 84896717675     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.12.013     Document Type: Article
Times cited : (49)

References (47)
  • 1
    • 77949508010 scopus 로고    scopus 로고
    • Quality control of protein standards for molecular mass determinations by small-angle X-ray scattering
    • S. Akiyama Quality control of protein standards for molecular mass determinations by small-angle X-ray scattering J. Appl. Cryst. 43 2010 237 243
    • (2010) J. Appl. Cryst. , vol.43 , pp. 237-243
    • Akiyama, S.1
  • 3
    • 84857570189 scopus 로고    scopus 로고
    • Structure, mechanism, and evolution of Ero1 family enzymes
    • K. Araki, and K. Inaba Structure, mechanism, and evolution of Ero1 family enzymes Antioxid. Redox Signal. 16 2012 790 799
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 790-799
    • Araki, K.1    Inaba, K.2
  • 5
  • 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
    • 58149215628 scopus 로고    scopus 로고
    • Insights into MHC class i peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer
    • G. Dong, P.A. Wearsch, D.R. Peaper, P. Cresswell, and K.M. Reinisch Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer Immunity 30 2009 21 32
    • (2009) Immunity , vol.30 , pp. 21-32
    • Dong, G.1    Wearsch, P.A.2    Peaper, D.R.3    Cresswell, P.4    Reinisch, K.M.5
  • 12
    • 84860289065 scopus 로고    scopus 로고
    • Structure of the third catalytic domain of the protein disulfide isomerase ERp46. Acta Crystallogr. F
    • I.E. Gulerez, G. Kozlov, A. Rosenauer, and K. Gehring Structure of the third catalytic domain of the protein disulfide isomerase ERp46. Acta Crystallogr. F Struct. Biol. & Crystalliz. Comm. 68 2012 378 381
    • (2012) Struct. Biol. & Crystalliz. Comm. , vol.68 , pp. 378-381
    • Gulerez, I.E.1    Kozlov, G.2    Rosenauer, A.3    Gehring, K.4
  • 14
    • 77957773053 scopus 로고    scopus 로고
    • Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI
    • K. Inaba, S. Masui, H. Iida, S. Vavassori, R. Sitia, and M. Suzuki Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI EMBO J. 29 2010 3330 3343
    • (2010) EMBO J. , vol.29 , pp. 3330-3343
    • Inaba, K.1    Masui, S.2    Iida, H.3    Vavassori, S.4    Sitia, R.5    Suzuki, M.6
  • 15
    • 70849101711 scopus 로고    scopus 로고
    • Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
    • C.E. Jessop, R.H. Watkins, J.J. Simmons, M. Tasab, and N.J. Bulleid Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins J. Cell Sci. 122 2009 4287 4295
    • (2009) J. Cell Sci. , vol.122 , pp. 4287-4295
    • Jessop, C.E.1    Watkins, R.H.2    Simmons, J.J.3    Tasab, M.4    Bulleid, N.J.5
  • 16
    • 64549156522 scopus 로고    scopus 로고
    • Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum
    • A.R. Karala, A.K. Lappi, M.J. Saaranen, and L.W. Ruddock Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum Antioxid. Redox Signal. 11 2009 963 970
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 963-970
    • Karala, A.R.1    Lappi, A.K.2    Saaranen, M.J.3    Ruddock, L.W.4
  • 19
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data. Acta crystallographica. Section D
    • A.G. Leslie The integration of macromolecular diffraction data. Acta crystallographica. Section D Biol. Crystallogr. 62 2006 48 57
    • (2006) Biol. Crystallogr. , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 20
    • 79955527426 scopus 로고    scopus 로고
    • Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI)
    • S. Masui, S. Vavassori, C. Fagioli, R. Sitia, and K. Inaba Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI) J. Biol. Chem. 286 2011 16261 16271
    • (2011) J. Biol. Chem. , vol.286 , pp. 16261-16271
    • Masui, S.1    Vavassori, S.2    Fagioli, C.3    Sitia, R.4    Inaba, K.5
  • 23
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method. Acta crystallographica. Section D
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method. Acta crystallographica. Section D Biol. Crystallogr. 53 1997 240 255
    • (1997) Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 25
    • 79952845544 scopus 로고    scopus 로고
    • Acceleration of disulfide-coupled protein folding using glutathione derivatives
    • M. Okumura, M. Saiki, H. Yamaguchi, and Y. Hidaka Acceleration of disulfide-coupled protein folding using glutathione derivatives FEBS J. 278 2011 1137 1144
    • (2011) FEBS J. , vol.278 , pp. 1137-1144
    • Okumura, M.1    Saiki, M.2    Yamaguchi, H.3    Hidaka, Y.4
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Carter Jr. Academic Press
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W. Carter Jr. Methods in Enzymology 1997 Academic Press 307 326
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • M.V. Petoukhov, and D.I. Svergun Global rigid body modeling of macromolecular complexes against small-angle scattering data Biophys. J. 89 2005 1237 1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 29
    • 84862548210 scopus 로고    scopus 로고
    • Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals
    • Y. Sato, and K. Inaba Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals FEBS J. 279 2012 2262 2271
    • (2012) FEBS J. , vol.279 , pp. 2262-2271
    • Sato, Y.1    Inaba, K.2
  • 32
    • 0344443678 scopus 로고    scopus 로고
    • EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor
    • D.C. Sullivan, L. Huminiecki, J.W. Moore, J.J. Boyle, R. Poulsom, D. Creamer, J. Barker, and R. Bicknell EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor J. Biol. Chem. 278 2003 47079 47088
    • (2003) J. Biol. Chem. , vol.278 , pp. 47079-47088
    • Sullivan, D.C.1    Huminiecki, L.2    Moore, J.W.3    Boyle, J.J.4    Poulsom, R.5    Creamer, D.6    Barker, J.7    Bicknell, R.8
  • 33
    • 0026243243 scopus 로고
    • Mathematical, ethods in smail-angle scateering data analysis
    • D.I. Svergun Mathematical, ethods in smail-angle scateering data analysis J. Appl. Cryst. 24 1991 485 492
    • (1991) J. Appl. Cryst. , vol.24 , pp. 485-492
    • Svergun, D.I.1
  • 34
    • 0026910457 scopus 로고
    • Determination of the regularrization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularrization parameter in indirect-transform methods using perceptual criteria J. Appl. Cryst. 25 1992 495 503
    • (1992) J. Appl. Cryst. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 35
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • D.I. Svergun, M.V. Petoukhov, and M.H. Koch Determination of domain structure of proteins from X-ray solution scattering Biophys. J. 80 2001 2946 2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 36
    • 78650270477 scopus 로고    scopus 로고
    • Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum
    • T.J. Tavender, J.J. Springate, and N.J. Bulleid Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum EMBO J. 29 2010 4185 4197
    • (2010) EMBO J. , vol.29 , pp. 4185-4197
    • Tavender, T.J.1    Springate, J.J.2    Bulleid, N.J.3
  • 37
    • 30344444015 scopus 로고    scopus 로고
    • The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
    • G. Tian, S. Xiang, R. Noiva, W.J. Lennarz, and H. Schindelin The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites Cell 124 2006 61 73
    • (2006) Cell , vol.124 , pp. 61-73
    • Tian, G.1    Xiang, S.2    Noiva, R.3    Lennarz, W.J.4    Schindelin, H.5
  • 38
    • 0030061006 scopus 로고    scopus 로고
    • Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine
    • K.W. Walker, M.M. Lyles, and H.F. Gilbert Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine Biochemistry 35 1996 1972 1980
    • (1996) Biochemistry , vol.35 , pp. 1972-1980
    • Walker, K.W.1    Lyles, M.M.2    Gilbert, H.F.3
  • 39
    • 58649096169 scopus 로고    scopus 로고
    • Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase
    • L. Wang, S.J. Li, A. Sidhu, L. Zhu, Y. Liang, R.B. Freedman, and C.C. Wang Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase J. Biol. Chem. 284 2009 199 206
    • (2009) J. Biol. Chem. , vol.284 , pp. 199-206
    • Wang, L.1    Li, S.J.2    Sidhu, A.3    Zhu, L.4    Liang, Y.5    Freedman, R.B.6    Wang, C.C.7
  • 40
    • 84862907646 scopus 로고    scopus 로고
    • Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a'
    • C. Wang, J. Yu, L. Huo, L. Wang, W. Feng, and C.C. Wang Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a' J. Biol. Chem. 287 2012 1139 1149
    • (2012) J. Biol. Chem. , vol.287 , pp. 1139-1149
    • Wang, C.1    Yu, J.2    Huo, L.3    Wang, L.4    Feng, W.5    Wang, C.C.6
  • 41
    • 84878866786 scopus 로고    scopus 로고
    • Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase
    • C. Wang, W. Li, J. Ren, J. Fang, H. Ke, W. Gong, W. Feng, and C.C. Wang Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase Antioxid. Redox Signal. 19 2013 36 45
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 36-45
    • Wang, C.1    Li, W.2    Ren, J.3    Fang, J.4    Ke, H.5    Gong, W.6    Feng, W.7    Wang, C.C.8
  • 42
    • 84887465759 scopus 로고    scopus 로고
    • Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1a to promote oxidative protein folding
    • 10.1089/ars.2013.5236
    • L. Wang, L. Zhang, Y. Niu, R. Sitia, and C.C. Wang Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1a to promote oxidative protein folding Antioxid. Redox Signal. 2013 10.1089/ars.2013.5236
    • (2013) Antioxid. Redox Signal.
    • Wang, L.1    Zhang, L.2    Niu, Y.3    Sitia, R.4    Wang, C.C.5
  • 43
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • J.S. Weissman, and P.S. Kim Reexamination of the folding of BPTI: predominance of native intermediates Science 253 1991 1386 1393
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 44
    • 0027270735 scopus 로고
    • Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
    • J.S. Weissman, and P.S. Kim Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase Nature 365 1993 185 188
    • (1993) Nature , vol.365 , pp. 185-188
    • Weissman, J.S.1    Kim, P.S.2
  • 45
    • 0028818785 scopus 로고
    • A kinetic explanation for the rearrangement pathway of BPTI folding
    • J.S. Weissman, and P.S. Kim A kinetic explanation for the rearrangement pathway of BPTI folding Nat. Struct. Biol. 2 1995 1123 1130
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1123-1130
    • Weissman, J.S.1    Kim, P.S.2
  • 46
    • 1642473164 scopus 로고    scopus 로고
    • Identification of a novel thioredoxin-related protein, PC-TRP, which is preferentially expressed in plasma cells
    • J. Wrammert, E. Källberg, and T. Leanderson Identification of a novel thioredoxin-related protein, PC-TRP, which is preferentially expressed in plasma cells Eur. J. Immunol. 34 2004 137 146
    • (2004) Eur. J. Immunol. , vol.34 , pp. 137-146
    • Wrammert, J.1    Källberg, E.2    Leanderson, T.3
  • 47
    • 0035209087 scopus 로고    scopus 로고
    • Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering
    • W. Wriggers, and P. Chacon Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering J. Appl. Cryst. 34 2001 773 776
    • (2001) J. Appl. Cryst. , vol.34 , pp. 773-776
    • Wriggers, W.1    Chacon, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.