Recent advances in the high resolution structures of bacterial channels: Gramicidin A

被引:150
作者
Wallace, BA [1 ]
机构
[1] Univ London Birkbeck Coll, Dept Crystallog, London WC1E 7HX, England
关键词
circular dichroism spectroscopy; conductance; ion channels; membranes; NMR spectroscopy; phospholipid bilayers; pores; structure/function relationship; X-ray crystallography;
D O I
10.1006/jsbi.1997.3948
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
Gramicidin is a polypeptide antibiotic which forms dimeric channels specific for the transport of monovalent cations across membranes. It adopts several different conformations, most notably double helical (pore) and helical dimer (channels) forms, which have very different structural and functional characteristics. This review focuses on recent high resolution structure determinations of both the pore and channel forms of the molecule by X-ray crystallographic and/or NMR spectroscopic techniques. It discusses the structural consequences of binding ions and the location of ion binding sites and how the structures are related to the conductance;properties of the molecule. This relatively simple molecule is probably the best characterized ion channel (both structurally and functionally) and has, to date, been the principal proving-ground for many of our ideas about the molecular nature of ion conduction in membranes. (C) 1998 Academic Press.
引用
收藏
页码:123 / 141
页数:19
相关论文
共 117 条
[1]  
ANDERSEN OS, 1990, BIOPHYS J, V57, pA100
[2]  
ANDERSEN OS, 1989, METHOD ENZYMOL, V171, P62
[3]   ENERGETICS OF ION PERMEATION THROUGH MEMBRANE CHANNELS - SOLVATION OF NA+ BY GRAMICIDIN-A [J].
AQVIST, J ;
WARSHEL, A .
BIOPHYSICAL JOURNAL, 1989, 56 (01) :171-182
[4]   H-1-NMR STUDY OF GRAMICIDIN-A TRANSMEMBRANE ION CHANNEL - HEAD-TO-HEAD RIGHT-HANDED, SINGLE-STRANDED HELICES [J].
ARSENIEV, AS ;
BARSUKOV, IL ;
BYSTROV, VF ;
LOMIZE, AL ;
OVCHINNIKOV, YA .
FEBS LETTERS, 1985, 186 (02) :168-174
[5]   NMR SOLUTION STRUCTURE OF GRAMICIDIN-A COMPLEX WITH CESIUM CATIONS [J].
ARSENIEV, AS ;
BARSUKOV, IL ;
BYSTROV, VF .
FEBS LETTERS, 1985, 180 (01) :33-39
[6]   Conformational trapping in a membrane environment: A regulatory mechanism for protein activity? [J].
Arumugam, S ;
Pascal, S ;
North, CL ;
Hu, W ;
Lee, KC ;
Cotten, M ;
Ketchem, RR ;
Xu, F ;
Brenneman, M ;
Kovacs, F ;
Tian, F ;
Wang, A ;
Huo, S ;
Cross, TA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (12) :5872-5876
[7]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[8]   CHANNEL FORMATION KINETICS OF GRAMICIDIN-A IN LIPID BILAYER MEMBRANES [J].
BAMBERG, E ;
LAUGER, P .
JOURNAL OF MEMBRANE BIOLOGY, 1973, 11 (02) :177-194
[9]   STRUCTURE OF GRAMICIDIN A CHANNEL - DISCRIMINATION BETWEEN PI-L,D AND BETA-HELIX BY ELECTRICAL MEASUREMENTS WITH LIPID BILAYER MEMBRANES [J].
BAMBERG, E ;
APELL, HJ ;
ALPES, H .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1977, 74 (06) :2402-2406
[10]   CONFORMATIONAL TRANSITIONS OF GRAMICIDIN A IN PHOSPHOLIPID MODEL MEMBRANES - A HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY ASSESSMENT [J].
BANO, MC ;
BRACO, L ;
ABAD, C .
BIOCHEMISTRY, 1991, 30 (04) :886-894