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Volumn 12, Issue 1, 2011, Pages

Delineation of the Pasteurellaceae-specific GbpA-family of glutathione-binding proteins

Author keywords

ABC transporter; DppA; GbpA; glutathione; HbpA; SBP; solute binding protein

Indexed keywords

BINDING PROTEIN; DIPEPTIDE; GLUTATHIONE; HEME BINDING PROTEIN A; HEMIN; LIPOPROTEIN; PROTEIN GBPA; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARRIER PROTEIN; GLUTATHIONE TRANSPORTER;

EID: 81055138859     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-12-59     Document Type: Article
Times cited : (8)

References (30)
  • 1
    • 0026621245 scopus 로고
    • ABC Transporters: From microorganisms to man
    • ABC transporters: from microorganisms to man. Higgins CF, Annu Rev Cell Biol 1992 8 67 113 10.1146/annurev.cb.08.110192.000435 1282354 (Pubitemid 23000992)
    • (1992) Annual Review of Cell Biology , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 80052436005 scopus 로고    scopus 로고
    • Conformational Coupling of the Nucleotide-Binding and the Transmembrane Domains in ABC Transporters
    • 10.1016/j.bpj.2011.06.031 21806936
    • Conformational Coupling of the Nucleotide-Binding and the Transmembrane Domains in ABC Transporters. Wen PC, Tajkhorshid E, Biophys J 2011 101 680 690 10.1016/j.bpj.2011.06.031 21806936
    • (2011) Biophys J , vol.101 , pp. 680-690
    • Wen, P.C.1    Tajkhorshid, E.2
  • 3
    • 79957932347 scopus 로고    scopus 로고
    • Crystal structure of the maltose transporter in a pretranslocation intermediate state
    • 10.1126/science.1200767 21566157
    • Crystal structure of the maltose transporter in a pretranslocation intermediate state. Oldham ML, Chen J, Science 2011 332 1202 1205 10.1126/science.1200767 21566157
    • (2011) Science , vol.332 , pp. 1202-1205
    • Oldham, M.L.1    Chen, J.2
  • 4
    • 0036774002 scopus 로고    scopus 로고
    • ABC transporters: One, two or four extracytoplasmic substrate-binding sites?
    • DOI 10.1093/embo-reports/kvf201
    • ABC transporters: one, two or four extracytoplasmic substrate-binding sites? van der Heide T, Poolman B, EMBO Rep 2002 3 938 943 10.1093/embo-reports/ kvf201 12370206 (Pubitemid 35256467)
    • (2002) EMBO Reports , vol.3 , Issue.10 , pp. 938-943
    • Van Der Heide, T.1    Poolman, B.2
  • 5
    • 0026629422 scopus 로고
    • The hbpA gene of Haemophilus influenzae type b encodes a heme-binding lipoprotein conserved among heme-dependent Haemophilus species
    • 1339409
    • The hbpA gene of Haemophilus influenzae type b encodes a heme-binding lipoprotein conserved among heme-dependent Haemophilus species. Hanson MS, Slaughter C, Hansen EJ, Infect Immun 1992 60 2257 2266 1339409
    • (1992) Infect Immun , vol.60 , pp. 2257-2266
    • Hanson, M.S.1    Slaughter, C.2    Hansen, E.J.3
  • 6
    • 33947581907 scopus 로고    scopus 로고
    • Comparison of the localization and post-translational modification of Campylobacter coli CjaC and its homolog from Campylobacter jejuni, Cj0734c/HisJ
    • Comparison of the localization and post-translational modification of Campylobacter coli CjaC and its homolog from Campylobacter jejuni, Cj0734c/HisJ. Wyszynska A, Tomczyk K, Jagusztyn-Krynicka EK, Acta Biochim Pol 2007 54 143 150 17351673 (Pubitemid 46481827)
    • (2007) Acta Biochimica Polonica , vol.54 , Issue.1 , pp. 143-150
    • Wyszynska, A.1    Tomczyk, K.2    Jagusztyn-Krynicka, E.K.3
  • 7
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Tam R, Saier MH Jr, Microbiol Rev 1993 57 320 346 8336670 (Pubitemid 23170095)
    • (1993) Microbiological Reviews , vol.57 , Issue.2 , pp. 320-346
    • Tam, R.1    Saier Jr., M.H.2
  • 8
    • 77955828073 scopus 로고    scopus 로고
    • Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA
    • 10.1073/pnas.1005198107 20628015
    • Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA. Vergauwen B, Elegheert J, Dansercoer A, Devreese B, Savvides SN, Proc Natl Acad Sci USA 2010 107 13270 13275 10.1073/pnas.1005198107 20628015
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13270-13275
    • Vergauwen, B.1    Elegheert, J.2    Dansercoer, A.3    Devreese, B.4    Savvides, S.N.5
  • 9
    • 0020478556 scopus 로고
    • Hinge-bending in L-arabinose-binding protein. The "venus's- flytrap" model
    • 7035444
    • Hinge-bending in L-arabinose-binding protein. The "Venus's- flytrap" model. Mao B, Pear MR, McCammon JA, Quiocho FA, J Biol Chem 1982 257 1131 1133 7035444
    • (1982) J Biol Chem , vol.257 , pp. 1131-1133
    • Mao, B.1    Pear, M.R.2    McCammon, J.A.3    Quiocho, F.A.4
  • 10
    • 27944450784 scopus 로고    scopus 로고
    • The heme-binding lipoprotein (HbpA) of Haemophilus influenzae: Role in heme utilization
    • DOI 10.1016/j.femsle.2005.09.016, PII S0378109705006506
    • The heme-binding lipoprotein (HbpA) of Haemophilus influenzae: role in heme utilization. Morton DJ, Madore LL, Smith A, Vanwagoner TM, Seale TW, Whitby PW, Stull TL, FEMS Microbiol Lett 2005 253 193 199 10.1016/j.femsle.2005.09.016 16289530 (Pubitemid 41674515)
    • (2005) FEMS Microbiology Letters , vol.253 , Issue.2 , pp. 193-199
    • Morton, D.J.1    Madore, L.L.2    Smith, A.3    VanWagoner, T.M.4    Seale, T.W.5    Whitby, P.W.6    Stull, T.L.7
  • 13
    • 39749143945 scopus 로고    scopus 로고
    • The yejABEF operon of Salmonella confers resistance to antimicrobial peptides and contributes to its virulence
    • DOI 10.1099/mic.0.2007/011114-0
    • The yejABEF operon of Salmonella confers resistance to antimicrobial peptides and contributes to its virulence. Eswarappa SM, Panguluri KK, Hensel M, Chakravortty D, Microbiology 2008 154 666 678 10.1099/mic.0.2007/011114-0 18227269 (Pubitemid 351292319)
    • (2008) Microbiology , vol.154 , Issue.2 , pp. 666-678
    • Eswarappa, S.M.1    Panguluri, K.K.2    Hensel, M.3    Chakravortty, D.4
  • 14
    • 33748053969 scopus 로고    scopus 로고
    • The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins
    • DOI 10.1073/pnas.0605440103
    • The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins. Letoffe S, Delepelaire P, Wandersman C, Proc Natl Acad Sci USA 2006 103 12891 12896 10.1073/pnas.0605440103 16905647 (Pubitemid 44298657)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.34 , pp. 12891-12896
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 15
    • 77957886088 scopus 로고    scopus 로고
    • An oligopeptide transporter of Mycobacterium tuberculosis regulates cytokine release and apoptosis of infected macrophages
    • 10.1371/journal.pone.0012225 20808924
    • An oligopeptide transporter of Mycobacterium tuberculosis regulates cytokine release and apoptosis of infected macrophages. Dasgupta A, Sureka K, Mitra D, Saha B, Sanyal S, Das AK, Chakrabarti P, Jackson M, Gicquel B, Kundu M, Basu J, PLoS One 2010 5 12225 10.1371/journal.pone.0012225 20808924
    • (2010) PLoS One , vol.5 , pp. 512225
    • Dasgupta, A.1    Sureka, K.2    Mitra, D.3    Saha, B.4    Sanyal, S.5    Das, A.K.6    Chakrabarti, P.7    Jackson, M.8    Gicquel, B.9    Kundu, M.10    Basu, J.11
  • 16
    • 0028786979 scopus 로고
    • Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis
    • 10.1002/pro.5560041110 8563629
    • Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis. Dunten P, Mowbray SL, Protein Sci 1995 4 2327 2334 10.1002/pro.5560041110 8563629
    • (1995) Protein Sci , vol.4 , pp. 2327-2334
    • Dunten, P.1    Mowbray, S.L.2
  • 18
    • 0034011876 scopus 로고    scopus 로고
    • Status of glutathione and other thiols and disulfides in human plasma
    • DOI 10.1016/S0006-2952(00)00293-8, PII S0006295200002938
    • Status of glutathione and other thiols and disulfides in human plasma. Kleinman WA, Richie JP Jr, Biochem Pharmacol 2000 60 19 29 10.1016/S0006- 2952(00)00293-8 10807941 (Pubitemid 30243081)
    • (2000) Biochemical Pharmacology , vol.60 , Issue.1 , pp. 19-29
    • Kleinman, W.A.1    Richie Jr., J.P.2
  • 19
    • 79956142965 scopus 로고    scopus 로고
    • Heme utilization by nontypeable Haemophilus influenzae is essential and dependent on Sap transporter function
    • 10.1128/JB.01313-10 21441512
    • Heme utilization by nontypeable Haemophilus influenzae is essential and dependent on Sap transporter function. Mason KM, Raffel FK, Ray WC, Bakaletz LO, J Bacteriol 2011 193 2527 2535 10.1128/JB.01313-10 21441512
    • (2011) J Bacteriol , vol.193 , pp. 2527-2535
    • Mason, K.M.1    Raffel, F.K.2    Ray, W.C.3    Bakaletz, L.O.4
  • 20
    • 21244445047 scopus 로고    scopus 로고
    • An ATP-binding cassette-type cysteine transporter in Campylobacter jejuni inferred from the structure of an extracytoplasmic solute receptor protein
    • DOI 10.1111/j.1365-2958.2005.04691.x
    • An ATP-binding cassette-type cysteine transporter in Campylobacter jejuni inferred from the structure of an extracytoplasmic solute receptor protein. Muller A, Thomas GH, Horler R, Brannigan JA, Blagova E, Levdikov VM, Fogg MJ, Wilson KS, Wilkinson AJ, Mol Microbiol 2005 57 143 155 10.1111/j.1365-2958.2005. 04691.x 15948956 (Pubitemid 40896604)
    • (2005) Molecular Microbiology , vol.57 , Issue.1 , pp. 143-155
    • Muller, A.1    Thomas, G.H.2    Horler, R.3    Brannigan, J.A.4    Blagova, E.5    Levdikov, V.M.6    Fogg, M.J.7    Wilson, K.S.8    Wilkinson, A.J.9
  • 21
    • 10044241873 scopus 로고    scopus 로고
    • The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide
    • DOI 10.1016/j.jmb.2004.10.089, PII S002228360401410X
    • The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide. Levdikov VM, Blagova EV, Brannigan JA, Wright L, Vagin AA, Wilkinson AJ, J Mol Biol 2005 345 879 892 10.1016/j.jmb.2004.10.089 15588833 (Pubitemid 39600940)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.4 , 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
  • 22
    • 77956944744 scopus 로고    scopus 로고
    • Conformational changes and ligand recognition of Escherichia coli D-xylose binding protein revealed
    • 10.1016/j.jmb.2010.07.038 20678502
    • Conformational changes and ligand recognition of Escherichia coli D-xylose binding protein revealed. Sooriyaarachchi S, Ubhayasekera W, Park C, Mowbray SL, J Mol Biol 2010 402 657 668 10.1016/j.jmb.2010.07.038 20678502
    • (2010) J Mol Biol , vol.402 , pp. 657-668
    • Sooriyaarachchi, S.1    Ubhayasekera, W.2    Park, C.3    Mowbray, S.L.4
  • 23
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • 10.1016/0003-2697(76)90067-1 822747
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Thomas PE, Ryan D, Levin W, Anal Biochem 1976 75 168 176 10.1016/0003-2697(76) 90067-1 822747
    • (1976) Anal Biochem , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 26
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: A program for mutating pdb files used as templates in molecular replacement
    • DOI 10.1107/S0021889808006985, PII S0021889808006985
    • CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. Stein N, Journal of Applied Crystallography 2008 41 641 643 10.1107/S0021889808006985 (Pubitemid 351693895)
    • (2008) Journal of Applied Crystallography , vol.41 , Issue.3 , pp. 641-643
    • Stein, N.1
  • 30
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0
    • 10.1093/sysbio/syq010 20525638
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O, Syst Biol 2010 59 307 321 10.1093/sysbio/syq010 20525638
    • (2010) Syst Biol , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.