The structures of BtuCD and MscS and their implications for transporter and channel function

被引:23
作者
Bass, RB
Locher, KP
Borths, E
Poon, Y
Strop, P
Lee, A
Rees, DC [1 ]
机构
[1] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA
[2] CALTECH, Howard Hughes Med Inst, Pasadena, CA 91125 USA
关键词
transport protein; mechanosensitive channel; ATP binding cassette transporter; membrane protein structure;
D O I
10.1016/S0014-5793(03)01126-8
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
The passage of most molecules across biological membranes is mediated by specialized integral membrane proteins known as channels and transporters. Although these transport families encompass a wide range of functions, molecular architectures and mechanisms, there are common elements that must be incorporated within their structures, namely the translocation pathway, ligand specificity elements and regulatory sensors to control the rate of ligand flow across the membrane. This minireview discusses aspects of the structure and mechanism of two bacterial transport systems, the stretch-activated mechanosensitive channel of small conductance (MscS) and the ATP-dependent vitamin B12 uptake system (BtuCD), emphasizing their general implications for transporter function. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:111 / 115
页数:5
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