1OXS

Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus

1OXS の概要

• エントリーDOI: 10.2210/pdb1oxs/pdb
• 分子名称: ABC transporter, ATP binding protein, IODIDE ION (3 entities in total)
• 機能のキーワード: abc-atpase, atp-binding cassette, atpase, glcv, sulfolobus solfataricus, transport protein
• 由来する生物種: Sulfolobus solfataricus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42720.66

構造登録者

Verdon, G.,Albers, S.V.,Dijkstra, B.W.,Driessen, A.J.,Thunnissen, A.M. (登録日: 2003-04-03, 公開日: 2003-06-17, 最終更新日: 2024-02-14)

主引用文献

Verdon, G.,Albers, S.V.,Dijkstra, B.W.,Driessen, A.J.,Thunnissen, A.M.
Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations
J.Mol.Biol., 330:343-358, 2003

PubMed Abstract: 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-Mg(2+) as a product-bound state, and with AMPPNP-Mg(2+) 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-Mg(2+)-bound GlcV structure with that of the dimeric ATP-Na(+)-bound LolD-E171Q mutant reveals a +/-20 degrees rigid body re-orientation of the ABCalpha 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.

PubMed: 12823973
DOI: 10.1016/S0022-2836(03)00575-8

実験手法

X-RAY DIFFRACTION (1.65 Å)