ATP-binding cassette transporters in bacteria

被引:512
作者
Davidson, AL [1 ]
Chen, J
机构
[1] Baylor Coll Med, Dept Mol Virol & Microbiol, Houston, TX 77030 USA
[2] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
关键词
structure; transport; coupling; conformational change; efflux;
D O I
10.1146/annurev.biochem.73.011303.073626
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
ATP-binding cassette (ABC) transporters couple ATP hydrolysis to the uptake and efflux of solutes across the cell membrane in bacteria and eukaryotic cells. In bacteria, these transporters are important virulence factors because they play roles in nutrient uptake and in secretion of toxins and antimicrobial agents. In humans, many diseases, such as cystic fibrosis, hyperinsulinemia, and macular dystrophy, are traced to defects in ABC transporters. Recent advances in structural determination and functional analysis of bacterial ABC transporters, reviewed herein, have greatly increased our understanding of the molecular mechanism of transport in this transport superfamily.
引用
收藏
页码:241 / 268
页数:28
相关论文
共 134 条
[61]   Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export [J].
Koronakis, V ;
Sharff, A ;
Koronakis, E ;
Luisi, B ;
Hughes, C .
NATURE, 2000, 405 (6789) :914-919
[62]   PHYLOGENETIC ANALYSES OF THE ATP-BINDING CONSTITUENTS OF BACTERIAL EXTRACYTOPLASMIC RECEPTOR-DEPENDENT ABC-TYPE NUTRIENT-UPTAKE PERMEASES [J].
KUAN, G ;
DASSA, E ;
SAURIN, W ;
HOFNUNG, M ;
SAIER, MH .
RESEARCH IN MICROBIOLOGY, 1995, 146 (04) :271-278
[63]  
KUHNAU S, 1991, J BACTERIOL, V173, P2180
[64]   Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: Equilibrium, kinetic, and crystallographic studies [J].
Ledvina, PS ;
Tsai, AL ;
Wang, ZM ;
Koehl, E ;
Quiocho, FA .
PROTEIN SCIENCE, 1998, 7 (12) :2550-2559
[65]   Protein secretion in Gram-negative bacteria: Assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding [J].
Letoffe, S ;
Delepelaire, P ;
Wandersman, C .
EMBO JOURNAL, 1996, 15 (21) :5804-5811
[66]   ACTIVE EFFLUX MECHANISMS FOR ANTIMICROBIAL RESISTANCE [J].
LEVY, SB .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1992, 36 (04) :695-703
[67]   Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter) [J].
Liu, CE ;
Liu, PQ ;
Ames, GFL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (35) :21883-21891
[68]   Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains [J].
Liu, RH ;
Sharom, FJ .
BIOCHEMISTRY, 1996, 35 (36) :11865-11873
[69]   The E-coli BtuCD structure:: A framework for ABC transporter architecture and mechanism [J].
Locher, KP ;
Lee, AT ;
Rees, DC .
SCIENCE, 2002, 296 (5570) :1091-1098
[70]   COVALENT MODIFICATION OF HUMAN P-GLYCOPROTEIN MUTANTS CONTAINING A SINGLE CYSTEINE IN EITHER NUCLEOTIDE-BINDING FOLD ABOLISHES DRUG-STIMULATED ATPASE ACTIVITY [J].
LOO, TW ;
CLARKE, DM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (39) :22957-22961