Crystal Structures of the ATPase Subunit of the Glucose ABC Transporter from Sulfolobus solfataricus: Nucleotide-free and Nucleotide-bound Conformations

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• 作者：Verdon ; Gré ; gory ; Albers ; Sonja V. ; Dijkstra ; Bauke W. ; Driessen ; Arnold J.M. ; Thunnissen ; Andy-Mark W.H.
• 关键词：ABC-ATPase ; ATP-binding cassette ; conformational changes ; Q-loop ; X-ray crystallography ; ABC ; ATP-binding cassette
• 刊名：Journal of Molecular Biology
• 出版年：2003
• 出版时间：July 4, 2003
• 年：2003
• 卷：330
• 期：2
• 页码：343-358
• 全文大小：3.94 M

文摘

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 ABCα subdomain and the C-terminal domain relative to the ABCα/β 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 LolD-E171Q mutant reveals a ±20° rigid body re-orientation of the ABCα subdomain relative to the ABCα/β 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.