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Volumn 106, Issue 6, 2009, Pages 1778-1783

Erratum: The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter (Proceedings of the National Academy of Sciences of the United States of America (2009) 106:6 (1778-1783) DOI: 10.1073/pnas.0809979106);The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter

Author keywords

Haemophilus influenzae; Receptor dependent translocation; Sialic acid; SiaPQM; Tripartite ATP independent periplasmic transporter

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTEIN TRAP; SIALIC ACID DERIVATIVE; SODIUM; UNCLASSIFIED DRUG;

EID: 60549098063     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0809979106     Document Type: Erratum
Times cited : (77)

References (29)
  • 1
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson AL, Dassa E, Orelle C, Chen J (2008) Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol Mol Biol Rev 72:317-364.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 2
    • 31944431842 scopus 로고    scopus 로고
    • ABC transporter architecture and regulatory roles of accessory domains
    • Biemans-Oldehinkel E, Doeven MK, Poolman B (2006) ABC transporter architecture and regulatory roles of accessory domains. FEBS Lett 580:1023-1035.
    • (2006) FEBS Lett , vol.580 , pp. 1023-1035
    • Biemans-Oldehinkel, E.1    Doeven, M.K.2    Poolman, B.3
  • 3
    • 0036774002 scopus 로고    scopus 로고
    • ABC transporters: One, two or four extracytoplasmic substrate-binding sites?
    • van der Heide T, Poolman B (2002) ABC transporters: One, two or four extracytoplasmic substrate-binding sites? EMBO Rep 3:938-943.
    • (2002) EMBO Rep , vol.3 , pp. 938-943
    • van der Heide, T.1    Poolman, B.2
  • 4
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein K, Frei DC, Locher KP (2007) Structure of an ABC transporter in complex with its binding protein. Nature 446:213-216.
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 5
    • 1942532335 scopus 로고    scopus 로고
    • ABC transporter architecture and mechanism: Implications from the crystal structures of BtuCD and BtuF
    • Locher KP, Borths E (2004) ABC transporter architecture and mechanism: Implications from the crystal structures of BtuCD and BtuF. FEBS Lett 564:264-268.
    • (2004) FEBS Lett , vol.564 , pp. 264-268
    • Locher, K.P.1    Borths, E.2
  • 6
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham ML, Khare D, Quiocho FA, Davidson AL, 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
  • 7
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate-type ABC transporter
    • Pinkett HW, Lee AT, Lum P, Locher KP, Rees DC (2007) An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315:373-377.
    • (2007) Science , vol.315 , pp. 373-377
    • Pinkett, H.W.1    Lee, A.T.2    Lum, P.3    Locher, K.P.4    Rees, D.C.5
  • 8
    • 0030967906 scopus 로고    scopus 로고
    • TRAP transporters: A new family of periplasmic solute transport systems encoded by the dctPQM genes of Rhodobacter capsulatus and by homologs in diverse gram-negative bacteria
    • Forward JA, Behrendt MC, Wyborn NR, Cross R, Kelly DJ (1997) TRAP transporters: A new family of periplasmic solute transport systems encoded by the dctPQM genes of Rhodobacter capsulatus and by homologs in diverse gram-negative bacteria. J Bacteriol 179:5482-5493.
    • (1997) J Bacteriol , vol.179 , pp. 5482-5493
    • Forward, J.A.1    Behrendt, M.C.2    Wyborn, N.R.3    Cross, R.4    Kelly, D.J.5
  • 9
    • 0141852840 scopus 로고    scopus 로고
    • The tripartite tricarboxylate transporter (TTT) family
    • Winnen B, Hvorup RN, Saier MH, Jr. (2003) The tripartite tricarboxylate transporter (TTT) family. Res Microbiol 154:457-465.
    • (2003) Res Microbiol , vol.154 , pp. 457-465
    • Winnen, B.1    Hvorup, R.N.2    Saier Jr., M.H.3
  • 10
    • 0029843402 scopus 로고    scopus 로고
    • Glutamate transport in Rhodobacter sphaeroides is mediated by a novel binding protein-dependent secondary transport system
    • Jacobs MH, van der HT, Driessen AJ, Konings WN (1996) Glutamate transport in Rhodobacter sphaeroides is mediated by a novel binding protein-dependent secondary transport system. Proc Natl Acad Sci USA 93:12786-12790.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12786-12790
    • Jacobs1    MH, V.D.H.2    Driessen, A.J.3    Konings, W.N.4
  • 11
    • 0034889137 scopus 로고    scopus 로고
    • The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea
    • Kelly DJ, Thomas GH (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
  • 12
    • 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 DJ, Thomas GH (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
  • 14
    • 27944469933 scopus 로고    scopus 로고
    • Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporter
    • Severi E, et al. (2005) Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporter. Mol Microbiol 58:1173-1185.
    • (2005) Mol Microbiol , vol.58 , pp. 1173-1185
    • Severi, E.1
  • 15
    • 34948865783 scopus 로고    scopus 로고
    • Sialic acid utilization by bacterial pathogens
    • Severi E, Hood DW, Thomas GH (2007) Sialic acid utilization by bacterial pathogens. Microbiology 153:2817-2822.
    • (2007) Microbiology , vol.153 , pp. 2817-2822
    • Severi, E.1    Hood, D.W.2    Thomas, G.H.3
  • 16
    • 0042307333 scopus 로고    scopus 로고
    • Host-derived sialic acid is incorporated into Haemophilus influenzae lipopolysaccharide and is a major virulence factor in experimental otitis media
    • Bouchet V, et al. (2003) Host-derived sialic acid is incorporated into Haemophilus influenzae lipopolysaccharide and is a major virulence factor in experimental otitis media. Proc Natl Acad Sci USA 100:8898-8903.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8898-8903
    • Bouchet, V.1
  • 17
    • 33746848092 scopus 로고    scopus 로고
    • Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae
    • Muller A, et al. (2006) Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae. J Biol Chem 281:22212-22222.
    • (2006) J Biol Chem , vol.281 , pp. 22212-22222
    • Muller, A.1
  • 18
    • 38149082260 scopus 로고    scopus 로고
    • Characterization of the N-acetyl-5-neuraminic acid-binding site of the extracytoplasmic solute receptor (SiaP) of nontypeable Haemophilus influenzae strain 2019
    • Johnston JW, et al. (2008) Characterization of the N-acetyl-5-neuraminic acid-binding site of the extracytoplasmic solute receptor (SiaP) of nontypeable Haemophilus influenzae strain 2019. J Biol Chem 283:855-865.
    • (2008) J Biol Chem , vol.283 , pp. 855-865
    • Johnston, J.W.1
  • 19
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177:4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 20
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • de Ruyter PG, Kuipers OP, De Vos WM (1996) Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl Environ Microbiol 62:3662-3667.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3662-3667
    • de Ruyter, P.G.1    Kuipers, O.P.2    De Vos, W.M.3
  • 21
    • 18744433753 scopus 로고    scopus 로고
    • Expression of prokaryotic membrane transport proteins in Escherichia coli
    • Ward A, et al. (1999) Expression of prokaryotic membrane transport proteins in Escherichia coli. Biochem Soc Trans 27:893-899.
    • (1999) Biochem Soc Trans , vol.27 , pp. 893-899
    • Ward, A.1
  • 22
    • 0016615611 scopus 로고
    • Solubilization of bacterialmembraneproteins using alkyl glucosides and dioctanoyl phosphatidylcholine
    • Baron C, Thompson TE (1975) Solubilization of bacterialmembraneproteins using alkyl glucosides and dioctanoyl phosphatidylcholine. Biochim Biophys Acta 382:276-285.
    • (1975) Biochim Biophys Acta , vol.382 , pp. 276-285
    • Baron, C.1    Thompson, T.E.2
  • 23
    • 0027458057 scopus 로고
    • Secondary solute transport in bacteria
    • Poolman B, Konings WN (1993) Secondary solute transport in bacteria. Biochim Biophys Acta 1183:5-39.
    • (1993) Biochim Biophys Acta , vol.1183 , pp. 5-39
    • Poolman, B.1    Konings, W.N.2
  • 24
    • 0018306535 scopus 로고
    • Mechanism of lactose translocation in membrane vesicles from Escherichia coli. 1. Effect of pH on efflux, exchange, and counterflow
    • Kaczorowski GJ, Kaback HR (1979) Mechanism of lactose translocation in membrane vesicles from Escherichia coli. 1. Effect of pH on efflux, exchange, and counterflow. Biochemistry 18:3691-3697.
    • (1979) Biochemistry , vol.18 , pp. 3691-3697
    • Kaczorowski, G.J.1    Kaback, H.R.2
  • 25
    • 30744445718 scopus 로고    scopus 로고
    • Novel ligands for the extracellular solute receptors of two bacterial TRAP transporters
    • Thomas GH, Southworth T, Leon-Kempis MR, Leech A, Kelly DJ (2006) Novel ligands for the extracellular solute receptors of two bacterial TRAP transporters. Microbiology 152:187-198.
    • (2006) Microbiology , vol.152 , pp. 187-198
    • Thomas, G.H.1    Southworth, T.2    Leon-Kempis, M.R.3    Leech, A.4    Kelly, D.J.5
  • 26
    • 34047164005 scopus 로고    scopus 로고
    • Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding
    • Gonin S, et al. (2007) Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding. BMC Struct Biol 7:11.
    • (2007) BMC Struct Biol , vol.7 , pp. 11
    • Gonin, S.1
  • 27
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • Patzlaff JS, van der Heide T, Poolman B (2003) The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA. J Biol Chem 278:29546-29551.
    • (2003) J Biol Chem , vol.278 , pp. 29546-29551
    • Patzlaff, J.S.1    van der Heide, T.2    Poolman, B.3
  • 28
    • 34548319070 scopus 로고    scopus 로고
    • High-throughput cloning and expression in recalcitrant bacteria
    • Geertsma ER, Poolman B (2007) High-throughput cloning and expression in recalcitrant bacteria. Nat Methods 4:705-707.
    • (2007) Nat Methods , vol.4 , pp. 705-707
    • Geertsma, E.R.1    Poolman, B.2
  • 29
    • 0037450575 scopus 로고    scopus 로고
    • Lactococcus lactis as host for overproduction of functional membrane proteins
    • Kunji ER, Slotboom DJ, Poolman B (2003) Lactococcus lactis as host for overproduction of functional membrane proteins. Biochim Biophys Acta 1610:97-108.
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 97-108
    • Kunji, E.R.1    Slotboom, D.J.2    Poolman, B.3


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