1oxu

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spinqualitylabelsall models 1oxu, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1OXU is a Single protein structure of sequence from Sulfolobus solfataricus with MG, IOD and ADP as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations., Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM, J Mol Biol. 2003 Jul 4;330(2):343-58. PMID:12823973

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