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Volumn 181, Issue 3, 2001, Pages 215-224

A triple mutant, K319N/H322Q/E325Q, of the lactose permease cotransports H+ with thiodigalactoside

Author keywords

Cotransporter; Lactose permease; Sugar transporter; Symporter

Indexed keywords

HYDROGEN; LACTOSE; PERMEASE; SUGAR; THIOGLYCOSIDE;

EID: 0035365996     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-001-0024-2     Document Type: Article
Times cited : (13)

References (56)
  • 3
    • 0023825249 scopus 로고
    • Bioenergetic coupling to protonmotive force: Should we be considering hydronium ion coordination and not group protonation?
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 5-7
    • Boyer, P.D.1
  • 13
    • 0025765577 scopus 로고
    • An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. II. Second site revertants of the thiodigalactoside-dependent proton leak by the Val177/Asn319 permease
    • (1991) J. Biol. Chem. , vol.266 , pp. 4139-4144
    • Eelkema, J.A.1    O'Donnell, M.A.2    Brooker, R.J.3
  • 18
    • 0032740145 scopus 로고    scopus 로고
    • Arg-52 in the melibiose carrier of Escherichia coli is important for cation-coupled sugar transport and participates in an intrahelical salt bridge
    • (1999) J. Bacteriol. , vol.181 , pp. 6377-6386
    • Franco, P.J.1    Wilson, T.H.2
  • 23
    • 0028827716 scopus 로고
    • Use of designed metal-binding sites to study helix proximity in the lactose permease of Escherichia coli. 2. Proximity of helix IX (Arg302) with helix X (His322 and Glu325)
    • (1995) Biochemistry , vol.34 , pp. 15667-15670
    • He, M.M.1    Voss, J.2    Hubbell, W.L.3    Kaback, H.R.4
  • 25
    • 0030053616 scopus 로고    scopus 로고
    • Evidence that the conserved motif, G-X-X-X-D/E-R/K-X-G-[X]-R/K-R/K, in hydrophilic loop 2-3 affects a conformationally-sensitive interface between the two halves of the lactose permease
    • (1996) J. Biol. Chem. , vol.271 , pp. 1400-1404
    • Jessen-Marshall, A.E.1    Brooker, R.J.2
  • 28
    • 0030951324 scopus 로고    scopus 로고
    • A molecular mechanism for energy coupling in a membrane transport protein, the lactose permease of Escherichia coli
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5539-5543
    • Kaback, H.R.1
  • 40
    • 0027447867 scopus 로고
    • Mutagenesis of acidic residues in putative membrane-spanning segments of the melibiose permease of Escherichia coli. I. Effect on Na(+)-dependent transport and binding properties
    • (1993) J. Biol. Chem. , vol.268 , pp. 3209-3215
    • Pourcher, T.1    Zani, M.-L.2    Leblanc, G.3
  • 52
    • 0033588117 scopus 로고    scopus 로고
    • Proximity relationships between helices I and XI or XII in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking
    • (1999) J. Mol. Biol. , vol.291 , pp. 683-692
    • Wang, Q.1    Kaback, H.R.2
  • 53
    • 0033537639 scopus 로고    scopus 로고
    • Helix packing in the lactose permease of Escherichia coli determined by site-directed thiol crosslinking: Helix I is close to helices V and XI
    • (1999) Biochemistry , vol.38 , pp. 3120-3126
    • Wang, Q.1    Kaback, H.R.2
  • 56
    • 0027403918 scopus 로고
    • Mutagenesis of acidic residues in putative membrane-spanning segments of the melibiose permease of Escherichia coli. II. Effect on cationic selectivity and coupling properties
    • (1993) J. Biol. Chem. , vol.268 , pp. 3216-3221
    • Zani, M.-L.1    Pourcher, T.2    Leblanc, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.