1OXT

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

Summary for 1OXT

• Entry DOI: 10.2210/pdb1oxt/pdb
• Related: 1OXS 1OXU 1OXV
• Descriptor: ABC transporter, ATP binding protein (2 entities in total)
• Functional Keywords: abc-atpase, atp-binding cassette, atpase, glcv, sulfolobus solfataricus, transport protein
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 3
• Total formula weight: 117502.04

Authors

Verdon, G.,Albers, S.V.,Dijkstra, B.W.,Driessen, A.J.,Thunnissen, A.M. (deposition date: 2003-04-03, release date: 2003-06-17, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)