메뉴 건너뛰기




Volumn 70, Issue 3, 2008, Pages 900-914

TPR domain of NrfG mediates complex formation between heme lyase and formate-dependent nitrite reductase in Escherichia coli O157:H7

Author keywords

Cytochrome C; E. coli O157; Formate dependent nitrite reductase; Heme lyase; NrfA; NrfG; TPR

Indexed keywords

BACTERIAL PROTEIN; CYTOCHROME C; HEME LYASE; LYASE; NITRITE REDUCTASE; PROTEIN NRFG; UNCLASSIFIED DRUG;

EID: 38549150882     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21597     Document Type: Article
Times cited : (18)

References (46)
  • 3
    • 0013936383 scopus 로고    scopus 로고
    • Fujita T. Studies on soluble cytochromes in Enterobacteriaceae. I. Detection, purification, and properties of cytochrome c-552 in anaerobically grown cells. J Biochem 1966;60:204-215.
    • Fujita T. Studies on soluble cytochromes in Enterobacteriaceae. I. Detection, purification, and properties of cytochrome c-552 in anaerobically grown cells. J Biochem 1966;60:204-215.
  • 4
    • 0013945477 scopus 로고
    • Studies on soluble cytochromes in Enterobacteriaceae. II. Cytochromes b-562 and c-550
    • Fujita T. Studies on soluble cytochromes in Enterobacteriaceae. II. Cytochromes b-562 and c-550. J Biochem 1966;60:329-334.
    • (1966) J Biochem , vol.60 , pp. 329-334
    • Fujita, T.1
  • 5
    • 0030033752 scopus 로고    scopus 로고
    • Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm
    • Grove J, Tanapongpipat S, Thomas G, Griffiths L, Crooke H, Cole J. Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm. Mol Microbiol 1996;19:467-481.
    • (1996) Mol Microbiol , vol.19 , pp. 467-481
    • Grove, J.1    Tanapongpipat, S.2    Thomas, G.3    Griffiths, L.4    Crooke, H.5    Cole, J.6
  • 6
    • 0031895861 scopus 로고    scopus 로고
    • Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli
    • Eaves DJ, Grove J, Staudenmann W, James P, Poole RK, White SA, Griffiths I, Cole JA. Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli. Mol Microbiol 1998;28:205-216.
    • (1998) Mol Microbiol , vol.28 , pp. 205-216
    • Eaves, D.J.1    Grove, J.2    Staudenmann, W.3    James, P.4    Poole, R.K.5    White, S.A.6    Griffiths, I.7    Cole, J.A.8
  • 7
    • 0028811652 scopus 로고
    • Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
    • Berks BC, Ferguson SJ, Moir JW, Richardson DJ. Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim Biophys Acta 1995;1232:97-173.
    • (1995) Biochim Biophys Acta , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.3    Richardson, D.J.4
  • 8
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • Kranz R, Lill R, Goldman B, Bonnard G, Merchant S. Molecular mechanisms of cytochrome c biogenesis: three distinct systems. Mol Microbiol 1998;29:383-396.
    • (1998) Mol Microbiol , vol.29 , pp. 383-396
    • Kranz, R.1    Lill, R.2    Goldman, B.3    Bonnard, G.4    Merchant, S.5
  • 9
    • 0036671471 scopus 로고    scopus 로고
    • Cytochrome c maturation: A complex pathway for a simple task?
    • Thony-Meyer L. Cytochrome c maturation: a complex pathway for a simple task? Biochem Soc Trans 2002;30:633-638.
    • (2002) Biochem Soc Trans , vol.30 , pp. 633-638
    • Thony-Meyer, L.1
  • 11
    • 0028290650 scopus 로고
    • A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria
    • Hussain H, Grove J, Griffiths L, Busby S, Cole J. A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria. Mol Microbiol 1994;12:153-163.
    • (1994) Mol Microbiol , vol.12 , pp. 153-163
    • Hussain, H.1    Grove, J.2    Griffiths, L.3    Busby, S.4    Cole, J.5
  • 12
    • 0029843893 scopus 로고    scopus 로고
    • The role of the genes nrf EFG and ccmFH in cytochrome c biosynthesis in Escherichia coli
    • Grove J, Busby S, Cole J. The role of the genes nrf EFG and ccmFH in cytochrome c biosynthesis in Escherichia coli. Mol Gen Genet 1996;252:332-341.
    • (1996) Mol Gen Genet , vol.252 , pp. 332-341
    • Grove, J.1    Busby, S.2    Cole, J.3
  • 13
    • 0037040888 scopus 로고    scopus 로고
    • A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c
    • Ren Q, Ahuja U, Thony-Meyer L. A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c. J Biol Chem 2002;277:7657-7663.
    • (2002) J Biol Chem , vol.277 , pp. 7657-7663
    • Ren, Q.1    Ahuja, U.2    Thony-Meyer, L.3
  • 14
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • D'Andrea LD, Regan L. TPR proteins: the versatile helix. Trends Biochem Sci 2003;28:655-662.
    • (2003) Trends Biochem Sci , vol.28 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 15
    • 11444265536 scopus 로고    scopus 로고
    • The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold
    • Wilson CG, Kajander T, Regan L. The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold. FEBS J 2005;272:166-179.
    • (2005) FEBS J , vol.272 , pp. 166-179
    • Wilson, C.G.1    Kajander, T.2    Regan, L.3
  • 16
    • 0025159176 scopus 로고
    • A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis
    • Sikorski RS, Boguski MS, Goebl M, Hieter P. A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis. Cell 1990;60:307-317.
    • (1990) Cell , vol.60 , pp. 307-317
    • Sikorski, R.S.1    Boguski, M.S.2    Goebl, M.3    Hieter, P.4
  • 17
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • Das AK, Cohen PW, Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J 1998;17:1192-1199.
    • (1998) EMBO J , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 18
    • 4744365127 scopus 로고    scopus 로고
    • Beyond consensus: Statistical free energies reveal hidden interactions in the design of a TPR motif
    • Magliery TJ, Regan L. Beyond consensus: statistical free energies reveal hidden interactions in the design of a TPR motif. J Mol Biol 2004;343:731-745.
    • (2004) J Mol Biol , vol.343 , pp. 731-745
    • Magliery, T.J.1    Regan, L.2
  • 19
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. Solvent content of protein crystals. J Mol Biol 1968;33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 20
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger TC, Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr 1999;55:849-861.
    • (1999) Acta Crystallogr , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 21
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger TC. Maximum-likelihood density modification. Acta Crystallogr 2000;56:965-972.
    • (2000) Acta Crystallogr , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 22
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger TC. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr 2003; 59:38-44.
    • (2003) Acta Crystallogr , vol.59 , pp. 38-44
    • Terwilliger, T.C.1
  • 23
    • 2142689200 scopus 로고    scopus 로고
    • Solve and resolve: Automated structure solution, density modification and model building
    • Terwilliger T. Solve and resolve: automated structure solution, density modification and model building. J Synchrotron Radiat 2004; 11:49-52.
    • (2004) J Synchrotron Radiat , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47 (Part 2): 110-119.
    • (1991) Acta Crystallogr A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 25
    • 0030498233 scopus 로고    scopus 로고
    • xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets
    • Kleywegt GJ, Jones TA. xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets. Acta Crystallogr 1996;52:826-828.
    • (1996) Acta Crystallogr , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 26
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr 2004;60:2126-2132.
    • (2004) Acta Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 27
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn MD, Isupov MN, Murshudov GN. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr 2001;57:122-133.
    • (2001) Acta Crystallogr , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 29
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 30
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - a program to identify and analyze structural motifs in proteins
    • Hutchinson EG, Thornton JM. PROMOTIF - a program to identify and analyze structural motifs in proteins. Protein Sci 1996;5:212-220.
    • (1996) Protein Sci , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 31
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • Chen R, Li L, Weng Z. ZDOCK: an initial-stage protein-docking algorithm. Proteins 2003;52:80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 32
    • 30544453079 scopus 로고    scopus 로고
    • Crystal structure of PilF: Functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa
    • Kim K, Oh J, Han D, Kim EE, Lee B, Kim Y. Crystal structure of PilF: functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa. Biochem Biophys Res Commun 2006;340: 1028-1038.
    • (2006) Biochem Biophys Res Commun , vol.340 , pp. 1028-1038
    • Kim, K.1    Oh, J.2    Han, D.3    Kim, E.E.4    Lee, B.5    Kim, Y.6
  • 33
    • 17644425688 scopus 로고    scopus 로고
    • Local and long-range stability in tandemly arrayed tetratricopeptide repeats
    • Main ER, Stott K, Jackson SE, Regan L. Local and long-range stability in tandemly arrayed tetratricopeptide repeats. Proc Natl Acad Sci USA 2005;102:5721-5726.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5721-5726
    • Main, E.R.1    Stott, K.2    Jackson, S.E.3    Regan, L.4
  • 34
    • 0037648552 scopus 로고    scopus 로고
    • Design of stable α-helical arrays from an idealized TPR motif
    • Main ER, Xiong Y, Cocco MJ, D'Andrea L, Regan L. Design of stable α-helical arrays from an idealized TPR motif. Structure 2003;11:497-508.
    • (2003) Structure , vol.11 , pp. 497-508
    • Main, E.R.1    Xiong, Y.2    Cocco, M.J.3    D'Andrea, L.4    Regan, L.5
  • 35
    • 4744341309 scopus 로고    scopus 로고
    • The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α
    • Jinek M, Rehwinkel J, Lazarus BD, Izaurralde E, Hanover JA, Conti E. The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α. Nat Struct Mol Biol 2004;11:1001-1007.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1001-1007
    • Jinek, M.1    Rehwinkel, J.2    Lazarus, B.D.3    Izaurralde, E.4    Hanover, J.A.5    Conti, E.6
  • 36
    • 0033664345 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5
    • Gatto GJ, Jr, Geisbrecht BV, Gould SJ, Berg JM. Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5. Nat Struct Biol 2000;7:1091-1095.
    • (2000) Nat Struct Biol , vol.7 , pp. 1091-1095
    • Gatto Jr, G.J.1    Geisbrecht, B.V.2    Gould, S.J.3    Berg, J.M.4
  • 37
    • 0035896043 scopus 로고    scopus 로고
    • An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei
    • Kumar A, Roach C, Hirsh IS, Turley S, deWalque S, Michels PA, Hol WG. An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei. J Mol Biol 2001;307:271-282.
    • (2001) J Mol Biol , vol.307 , pp. 271-282
    • Kumar, A.1    Roach, C.2    Hirsh, I.S.3    Turley, S.4    deWalque, S.5    Michels, P.A.6    Hol, W.G.7
  • 40
    • 0034671914 scopus 로고    scopus 로고
    • Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and hemepacking motifs
    • Einsle O, Stach P, Messerschmidt A, Simon J, Kroger A, Huber R, Kroneck PM. Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and hemepacking motifs. J Biol Chem 2000;275:39608-39616.
    • (2000) J Biol Chem , vol.275 , pp. 39608-39616
    • Einsle, O.1    Stach, P.2    Messerschmidt, A.3    Simon, J.4    Kroger, A.5    Huber, R.6    Kroneck, P.M.7
  • 41
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000;101:199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 42
    • 27944495299 scopus 로고    scopus 로고
    • Chaperoned ubiquitylation - crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex
    • Zhang M, Windheim M, Roe SM, Peggie M, Cohen P, Prodromou C, Pearl LH. Chaperoned ubiquitylation - crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex. Mol Cell 2005;20:525-538.
    • (2005) Mol Cell , vol.20 , pp. 525-538
    • Zhang, M.1    Windheim, M.2    Roe, S.M.3    Peggie, M.4    Cohen, P.5    Prodromou, C.6    Pearl, L.H.7
  • 43
    • 33846611978 scopus 로고    scopus 로고
    • TPRpred: A tool for prediction of TPR-, PPR- and SEL1-like repeats from protein sequences
    • Karpenahalli MR, Lupas AN, Soding J. TPRpred: a tool for prediction of TPR-, PPR- and SEL1-like repeats from protein sequences. BMC Bioinformatics 2007;8:2.
    • (2007) BMC Bioinformatics , vol.8 , pp. 2
    • Karpenahalli, M.R.1    Lupas, A.N.2    Soding, J.3
  • 44
    • 0036273999 scopus 로고    scopus 로고
    • The nrfI gene is essential for the attachment of the active site haem group of Wolinella succinogenes cytochrome c nitrite reductase
    • Pisa R, Stein T, Eichler R, Gross R, Simon J. The nrfI gene is essential for the attachment of the active site haem group of Wolinella succinogenes cytochrome c nitrite reductase. Mol Microbiol 2002;43: 763-770.
    • (2002) Mol Microbiol , vol.43 , pp. 763-770
    • Pisa, R.1    Stein, T.2    Eichler, R.3    Gross, R.4    Simon, J.5
  • 45
    • 1842687087 scopus 로고    scopus 로고
    • The roles of different regions of the CycH protein in c-type cytochrome biogenesis in Sinorhizobium meliloti
    • Cinege G, Kereszt A, Kertesz S, Balogh G, Dusha I. The roles of different regions of the CycH protein in c-type cytochrome biogenesis in Sinorhizobium meliloti. Mol Genet Genomics 2004;271:171-179.
    • (2004) Mol Genet Genomics , vol.271 , pp. 171-179
    • Cinege, G.1    Kereszt, A.2    Kertesz, S.3    Balogh, G.4    Dusha, I.5
  • 46
    • 0033032598 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation
    • Fabianek RA, Hofer T, Thony-Meyer L. Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation. Arch Microbiol 1999;171:92-100.
    • (1999) Arch Microbiol , vol.171 , pp. 92-100
    • Fabianek, R.A.1    Hofer, T.2    Thony-Meyer, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.