Structural diversity of ABC transporters

被引：282
|
作者：
ter Beek, Josy [1 ]
Guskov, Albert [1 ]
Slotboom, Dirk Jan [1 ]
机构：
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Biochem, NL-9747 AG Groningen, Netherlands
来源：
JOURNAL OF GENERAL PHYSIOLOGY | 2014年 / 143卷 / 04期
基金：
欧洲研究理事会;
关键词：
BINDING CASSETTE TRANSPORTER; COUPLING FACTOR TRANSPORTER; INWARD-FACING CONFORMATION; ATP-BINDING; ESCHERICHIA-COLI; MALTOSE TRANSPORTER; CRYSTAL-STRUCTURE; P-GLYCOPROTEIN; ALTERNATING ACCESS; MEMBRANE-PROTEINS;
D O I：
10.1085/jgp.201411164
中图分类号：
Q4 [生理学];
学科分类号：
071003 ;
摘要：
ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally related in all ABC transporters, the membrane-embedded domains, where the substrates are translocated, adopt four different unrelated folds. Here, we review the structural characteristics of ABC transporters and discuss the implications of this structural diversity for mechanistic diversity.
引用
收藏
页码：419 / 435
页数：17
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