Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus:: Nucleotide-free and nucleotide-bound conformations

被引:132
作者
Verdon, G
Albers, SV
Dijkstra, BW
Driessen, AJM
Thunnissen, AMWH
机构
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Biophys Chem Lab, NL-9747 AG Groningen, Netherlands
[2] Univ Groningen, Dept Microbiol, Groningen Biomol Sci & Biotechnol Inst, NL-9751 NN Haren, Netherlands
关键词
ABC-ATPase; ATP-binding cassette; conformational changes; Q-loop; X-ray crystallography;
D O I
10.1016/S0022-2836(03)00575-8
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 ABC-ATPase GlcV energizes a binding protein-dependent ABC transporter that mediates glucose uptake in Sulfolobus solfataricus. Here, we report high-resolution crystal structures of GlcV in different states along its catalytic cycle: distinct monomeric nucleotide-free states and monomeric complexes with ADP-Mg2+ as a product-bound state, and with AMPPNP-Mg2+ as an ATP-like bound state. The structure of GlcV consists of a typical ABC-ATPase domain, comprising two subdomains, connected by a linker region to a C-terminal domain of unknown function. Comparisons of the nucleotide-free and nucleotide-bound structures of GlcV reveal re-orientations of the ABCalpha subdomain and the C-terminal domain relative to the ABCalpha/beta subdomain, and switch-like rearrangements in the P-loop and Q-loop regions. Additionally, large conformational differences are observed between the GlcV structures and those of other ABC-ATPases, further emphasizing the inherent flexibility of these proteins. Notably, a comparison of the monomeric AMPPNP-Mg2+-bound GlcV structure with that of the,dimeric ATP-Na+-bound LoID-EI71Q mutant reveals a +/-20degrees rigid body re-orientation of theABCalpha subdomain relative to the ABCalpha/beta subdomain, accompanied by a local conformational difference in the Q-loop. We propose that these differences represent conformational changes that may have a role in the mechanism of energy-transduction and/or allosteric control of the ABC-ATPase activity in bacterial importers. (C) 2003 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:343 / 358
页数:16
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