메뉴 건너뛰기




Volumn 21, Issue 8, 2014, Pages 728-731

Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; MODELS, MOLECULAR; SHEWANELLA; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY; SYMPORTERS;

EID: 84905656444     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2860     Document Type: Article
Times cited : (72)

References (28)
  • 2
    • 84870180803 scopus 로고    scopus 로고
    • Recent advances in structural biology of peptide transporters
    • Terada, T. & Inui, K. Recent advances in structural biology of peptide transporters. Curr. Top. Membr. 70, 257-274 (2012
    • (2012) Curr. Top. Membr , vol.70 , pp. 257-274
    • Terada, T.1    Inui, K.2
  • 4
    • 79952738070 scopus 로고    scopus 로고
    • The alternating-Access mechanism of MFS transporters arises from inverted-Topology repeats
    • Radestock, S. & Forrest, L.R. The alternating-Access mechanism of MFS transporters arises from inverted-Topology repeats. J. Mol. Biol. 407, 698-715 (2011
    • (2011) J. Mol. Biol , vol.407 , pp. 698-715
    • Radestock, S.1    Forrest, L.R.2
  • 5
    • 84878896166 scopus 로고    scopus 로고
    • Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters
    • Quistgaard, E.M., Low, C., Moberg, P., Tresaugues, L. & Nordlund, P. Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters. Nat. Struct. Mol. Biol. 20, 766-768 (2013
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 766-768
    • Quistgaard, E.M.1    Low, C.2    Moberg, P.3    Tresaugues, L.4    Nordlund, P.5
  • 6
    • 0033759212 scopus 로고    scopus 로고
    • Whole genome analyses of transporters in spirochetes: Borrelia burgdorferi and Treponema pallidum
    • Saier, M.H. Jr. & Paulsen, I.T. Whole genome analyses of transporters in spirochetes: Borrelia burgdorferi and Treponema pallidum. J. Mol. Microbiol. Biotechnol. 2, 393-399 (2000
    • (2000) J. Mol. Microbiol. Biotechnol , vol.2 , pp. 393-399
    • Saier Jr., M.H.1    Paulsen, I.T.2
  • 7
    • 2342644210 scopus 로고    scopus 로고
    • Molecular and integrative physiology of intestinal peptide transport
    • Daniel, H. Molecular and integrative physiology of intestinal peptide transport. Annu. Rev. Physiol. 66, 361-384 (2004
    • (2004) Annu. Rev. Physiol , vol.66 , pp. 361-384
    • Daniel, H.1
  • 8
    • 0028179387 scopus 로고
    • The di-And tripeptide transport protein of lactococcus lactis a new type of bacterial peptide transporter
    • Hagting, A., Kunji, E.R., Leenhouts, K.J., Poolman, B. & Konings, W.N. The di-And tripeptide transport protein of Lactococcus lactis. A new type of bacterial peptide transporter. J. Biol. Chem. 269, 11391-11399 (1994
    • (1994) J. Biol. Chem , vol.269 , pp. 11391-11399
    • Hagting, A.1    Kunji, E.R.2    Leenhouts, K.J.3    Poolman, B.4    Konings, W.N.5
  • 9
    • 68149161029 scopus 로고    scopus 로고
    • Transport of drugs by proton-coupled peptide transporters: Pearls and pitfalls
    • Brandsch, M. Transport of drugs by proton-coupled peptide transporters: Pearls and pitfalls. Expert Opin. Drug Metab. Toxicol. 5, 887-905 (2009
    • (2009) Expert Opin. Drug Metab. Toxicol , vol.5 , pp. 887-905
    • Brandsch, M.1
  • 10
    • 84888192640 scopus 로고    scopus 로고
    • Drug transport via the intestinal peptide transporter PepT1
    • Brandsch, M. Drug transport via the intestinal peptide transporter PepT1. Curr. Opin. Pharmacol. 13, 881-887 (2013
    • (2013) Curr. Opin. Pharmacol , vol.13 , pp. 881-887
    • Brandsch, M.1
  • 11
    • 1442351172 scopus 로고    scopus 로고
    • Peptide transporters: Structure, function, regulation and application for drug delivery
    • Terada, T. & Inui, K. Peptide transporters: Structure, function, regulation and application for drug delivery. Curr. Drug Metab. 5, 85-94 (2004
    • (2004) Curr. Drug Metab , vol.5 , pp. 85-94
    • Terada, T.1    Inui, K.2
  • 12
    • 78751604619 scopus 로고    scopus 로고
    • Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters pept1 and pept2
    • Newstead, S. et al. Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2. EMBO J. 30, 417-426 (2011
    • (2011) EMBO J. , vol.30 , pp. 417-426
    • Newstead, S.1
  • 13
    • 84865237281 scopus 로고    scopus 로고
    • Alternating access mechanism in the POT family of oligopeptide transporters
    • Solcan, N. et al. Alternating access mechanism in the POT family of oligopeptide transporters. EMBO J. 31, 3411-3421 (2012
    • (2012) EMBO J. , vol.31 , pp. 3411-3421
    • Solcan, N.1
  • 14
    • 84883489166 scopus 로고    scopus 로고
    • Structural insights into substrate recognition in proton-dependent oligopeptide transporters
    • Guettou, F. et al. Structural insights into substrate recognition in proton-dependent oligopeptide transporters. EMBO Rep. 14, 804-810 (2013
    • (2013) EMBO Rep , vol.14 , pp. 804-810
    • Guettou, F.1
  • 15
    • 84879895875 scopus 로고    scopus 로고
    • Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT
    • Doki, S. et al. Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT. Proc. Natl. Acad. Sci. USA 110, 11343-11348 (2013
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 11343-11348
    • Doki, S.1
  • 16
    • 84875982058 scopus 로고    scopus 로고
    • High-Throughput analytical gel filtration screening of integral membrane proteins for structural studies
    • Löw, C. et al. High-Throughput analytical gel filtration screening of integral membrane proteins for structural studies. Biochim. Biophys. Acta 1830, 3497-3508 (2013
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3497-3508
    • Löw, C.1
  • 17
    • 0036024507 scopus 로고    scopus 로고
    • X-ray-induced debromination of nucleic acids at the Br K absorption edge and implications for MAD phasing
    • Ennifar, E., Carpentier, P., Ferrer, J.L., Walter, P. & Dumas, P. X-ray-induced debromination of nucleic acids at the Br K absorption edge and implications for MAD phasing. Acta Crystallogr. D Biol. Crystallogr. 58, 1262-1268 (2002
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 1262-1268
    • Ennifar, E.1    Carpentier, P.2    Ferrer, J.L.3    Walter, P.4    Dumas, P.5
  • 18
    • 34250826020 scopus 로고    scopus 로고
    • Using X-ray absorption spectra to monitor specific radiation damage to anomalously scattering atoms in macromolecular crystallography
    • Oliéric, V. et al. Using X-ray absorption spectra to monitor specific radiation damage to anomalously scattering atoms in macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 63, 759-768 (2007
    • (2007) Acta Crystallogr. D Biol. Crystallogr , vol.63 , pp. 759-768
    • Oliéric, V.1
  • 19
    • 0034004725 scopus 로고    scopus 로고
    • Kinetics and substrate specificity of membrane-reconstituted peptide transporter DtpT of Lactococcus lactis
    • Fang, G., Konings, W.N. & Poolman, B. Kinetics and substrate specificity of membrane-reconstituted peptide transporter DtpT of Lactococcus lactis. J. Bacteriol. 182, 2530-2535 (2000
    • (2000) J. Bacteriol , vol.182 , pp. 2530-2535
    • Fang, G.1    Konings, W.N.2    Poolman, B.3
  • 20
    • 84894520813 scopus 로고    scopus 로고
    • Analysing the substrate multispecificity of a proton-coupled oligopeptide transporter using a dipeptide library
    • Ito, K. et al. Analysing the substrate multispecificity of a proton-coupled oligopeptide transporter using a dipeptide library. Nat. Commun. 4, 2502 (2013
    • (2013) Nat. Commun , vol.4 , pp. 2502
    • Ito, K.1
  • 21
    • 84883489166 scopus 로고    scopus 로고
    • Structural insights into substrate recognition in proton-dependent oligopeptide transporters
    • Guettou, F. et al. Structural insights into substrate recognition in proton-dependent oligopeptide transporters. EMBO Rep. 14, 804-810 (2013
    • (2013) EMBO Rep , vol.14 , pp. 804-810
    • Guettou, F.1
  • 22
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong, M. et al. Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 103, 8060-8065 (2006
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8060-8065
    • Strong, M.1
  • 23
  • 24
    • 76449098262 scopus 로고    scopus 로고
    • Phenix: A comprehensive python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 25
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-Atom structure validation for macromolecular crystallography
    • Chen, V.B. et al. MolProbity: All-Atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12-21 (2010
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 26
    • 0032483039 scopus 로고    scopus 로고
    • Unidirectional reconstitution and characterization of purified na+/proline transporter of escherichia coli
    • Jung, H., Tebbe, S., Schmid, R. & Jung, K. Unidirectional reconstitution and characterization of purified Na+/proline transporter of Escherichia coli. Biochemistry 37, 11083-11088 (1998
    • (1998) Biochemistry , vol.37 , pp. 11083-11088
    • Jung, H.1    Tebbe, S.2    Schmid, R.3    Jung, K.4
  • 27
    • 0029897240 scopus 로고    scopus 로고
    • Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus
    • Knol, J. et al. Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus. J. Biol. Chem. 271, 15358-15366 (1996
    • (1996) J. Biol. Chem , vol.271 , pp. 15358-15366
    • Knol, J.1
  • 28
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of lowry et al which is more generally applicable
    • Peterson, G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83, 346-356 (1977
    • (1977) Anal. Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.