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Volumn 75, Issue 1, 2010, Pages 6-9

Homes for the orphans: Utilization of multiple substrate-binding proteins by ABC transporters: MicroCommentary

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; AMMONIUM DERIVATIVE; CARNITINE; HYDROLASE; NUCLEOTIDE BINDING PROTEIN;

EID: 72949123727     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06961.x     Document Type: Note
Times cited : (25)

References (17)
  • 1
    • 17544365410 scopus 로고    scopus 로고
    • Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases
    • Ames, G.F., Liu, C.E., Joshi, A.K. Nikaido, K. (1996) Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases. J Biol Chem 271 : 14264 14270.
    • (1996) J Biol Chem , vol.271 , pp. 14264-14270
    • Ames, G.F.1    Liu, C.E.2    Joshi, A.K.3    Nikaido, K.4
  • 2
    • 28944442871 scopus 로고    scopus 로고
    • In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B12 uptake
    • Borths, E.L., Poolman, B., Hvorup, R.N., Locher, K.P. Rees, D.C. (2005) In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B12 uptake. Biochemistry 44 : 16301 16309.
    • (2005) Biochemistry , vol.44 , pp. 16301-16309
    • Borths, E.L.1    Poolman, B.2    Hvorup, R.N.3    Locher, K.P.4    Rees, D.C.5
  • 3
    • 41949085567 scopus 로고    scopus 로고
    • Pseudomonas syringae BetT is a low-affinity choline transporter that is responsible for superior osmoprotection by choline over glycine betaine
    • Chen, C. Beattie, G.A. (2008) Pseudomonas syringae BetT is a low-affinity choline transporter that is responsible for superior osmoprotection by choline over glycine betaine. J Bacteriol 190 : 2717 2725.
    • (2008) J Bacteriol , vol.190 , pp. 2717-2725
    • Chen, C.1    Beattie, G.A.2
  • 4
    • 72949101439 scopus 로고    scopus 로고
    • The ATP-binding cassette transporter Cbc (choline/betaine/carnitine) recruits multiple substrate-binding proteins with strong specificity for distinct quaternary ammonium compounds
    • Chen, C., Malek, A.A., Wargo, M.J., Hogan, D.A. Beattie, G.A. (2009) The ATP-binding cassette transporter Cbc (choline/betaine/carnitine) recruits multiple substrate-binding proteins with strong specificity for distinct quaternary ammonium compounds. Mol Microbiol 75 : 29 45.
    • (2009) Mol Microbiol , vol.75 , pp. 29-45
    • Chen, C.1    Malek, A.A.2    Wargo, M.J.3    Hogan, D.A.4    Beattie, G.A.5
  • 5
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • table
    • Davidson, A.L., Dassa, E., Orelle, C. Chen, J. (2008) Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol Mol Biol Rev 72 : 317 364, table.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 6
    • 22644444206 scopus 로고    scopus 로고
    • Specificity and selectivity determinants of peptide transport in Lactococcus lactis and other microorganisms
    • Doeven, M.K., Kok, J. Poolman, B. (2005) Specificity and selectivity determinants of peptide transport in Lactococcus lactis and other microorganisms. Mol Microbiol 57 : 640 649.
    • (2005) Mol Microbiol , vol.57 , pp. 640-649
    • Doeven, M.K.1    Kok, J.2    Poolman, B.3
  • 7
    • 43849112947 scopus 로고    scopus 로고
    • Probing receptor-translocator interactions in the oligopeptide ABC transporter by fluorescence correlation spectroscopy
    • Doeven, M.K., van den Bogaart, G., Krasnikov, V. Poolman, B. (2008) Probing receptor-translocator interactions in the oligopeptide ABC transporter by fluorescence correlation spectroscopy. Biophys J 94 : 3956 3965.
    • (2008) Biophys J , vol.94 , pp. 3956-3965
    • Doeven, M.K.1    Van Den Bogaart, G.2    Krasnikov, V.3    Poolman, B.4
  • 8
    • 0034889137 scopus 로고    scopus 로고
    • The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea
    • Kelly, D.J. Thomas, G.H. (2001) The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea. FEMS Microbiol Rev 25 : 405 424.
    • (2001) FEMS Microbiol Rev , vol.25 , pp. 405-424
    • Kelly, D.J.1    Thomas, G.H.2
  • 9
    • 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. (2009) Alternating access in maltose transporter mediated by rigid-body rotations. Mol Cell 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
  • 10
    • 34250793938 scopus 로고    scopus 로고
    • Tripartite ATP-independent periplasmic transporters: Application of a relational database for genome-wide analysis of transporter gene frequency and organization
    • Mulligan, C., Kelly, D.J. Thomas, G.H. (2007) Tripartite ATP-independent periplasmic transporters: application of a relational database for genome-wide analysis of transporter gene frequency and organization. J Mol Microbiol Biotechnol 12 : 218 226.
    • (2007) J Mol Microbiol Biotechnol , vol.12 , pp. 218-226
    • Mulligan, C.1    Kelly, D.J.2    Thomas, G.H.3
  • 11
    • 60549098063 scopus 로고    scopus 로고
    • The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter
    • Mulligan, C., Geertsma, E.R., Severi, E., Kelly, D.J., Poolman, B. Thomas, G.H. (2009) The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter. Proc Natl Acad Sci USA 106 : 1778 1783.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1778-1783
    • Mulligan, C.1    Geertsma, E.R.2    Severi, E.3    Kelly, D.J.4    Poolman, B.5    Thomas, G.H.6
  • 12
    • 0033578760 scopus 로고    scopus 로고
    • One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease
    • Nikaido, K. Ames, G.F. (1999) One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease. J Biol Chem 274 : 26727 26735.
    • (1999) J Biol Chem , vol.274 , pp. 26727-26735
    • Nikaido, K.1    Ames, G.F.2
  • 13
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham, M.L., Khare, D., Quiocho, F.A., Davidson, A.L. Chen, J. (2007) Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450 : 515 521.
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 14
    • 51349104365 scopus 로고    scopus 로고
    • Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter
    • Orelle, C., Ayvaz, T., Everly, R.M., Klug, C.S. Davidson, A.L. (2008) Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter. Proc Natl Acad Sci USA 105 : 12837 12842.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 12837-12842
    • Orelle, C.1    Ayvaz, T.2    Everly, R.M.3    Klug, C.S.4    Davidson, A.L.5
  • 15
    • 0031886481 scopus 로고    scopus 로고
    • MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide l-alanyl-gamma-d-glutamyl-meso-diaminopimelate
    • Park, J.T., Raychaudhuri, D., Li, H., Normark, S. Mengin-Lecreulx, D. (1998) MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide l-alanyl-gamma-d-glutamyl-meso-diaminopimelate. J Bacteriol 180 : 1215 1223.
    • (1998) J Bacteriol , vol.180 , pp. 1215-1223
    • Park, J.T.1    Raychaudhuri, D.2    Li, H.3    Normark, S.4    Mengin-Lecreulx, D.5
  • 16
    • 33846040629 scopus 로고    scopus 로고
    • TransportDB: A comprehensive database resource for cytoplasmic membrane transport systems and outer membrane channels
    • Ren, Q., Chen, K. Paulsen, I.T. (2007) TransportDB: a comprehensive database resource for cytoplasmic membrane transport systems and outer membrane channels. Nucleic Acids Res 35 : D274 D279.
    • (2007) Nucleic Acids Res , vol.35
    • Ren, Q.1    Chen, K.2    Paulsen, I.T.3
  • 17
    • 0345730812 scopus 로고    scopus 로고
    • Analysis of differences in the functional properties of the substrate binding proteins of the Borrelia burgdorferi oligopeptide permease (Opp) operon
    • Wang, X.G., Kidder, J.M., Scagliotti, J.P., Klempner, M.S., Noring, R. Hu, L.T. (2004) Analysis of differences in the functional properties of the substrate binding proteins of the Borrelia burgdorferi oligopeptide permease (Opp) operon. J Bacteriol 186 : 51 60.
    • (2004) J Bacteriol , vol.186 , pp. 51-60
    • Wang, X.G.1    Kidder, J.M.2    Scagliotti, J.P.3    Klempner, M.S.4    Noring, R.5    Hu, L.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.