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- | [[Image:1oxu.jpg|left|200px]] | + | {{Seed}} |
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| {{STRUCTURE_1oxu| PDB=1oxu | SCENE= }} | | {{STRUCTURE_1oxu| PDB=1oxu | SCENE= }} |
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- | '''Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus'''
| + | ===Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus=== |
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- | ==Overview==
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- | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12823973}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 12823973 is the PubMed ID number. |
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| + | {{ABSTRACT_PUBMED_12823973}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Glcv]] | | [[Category: Glcv]] |
| [[Category: Sulfolobus solfataricus]] | | [[Category: Sulfolobus solfataricus]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:24:41 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:27:19 2008'' |
Revision as of 13:27, 27 July 2008
Template:STRUCTURE 1oxu
Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus
Template:ABSTRACT PUBMED 12823973
About this Structure
1OXU is a Single protein structure of sequence from Sulfolobus solfataricus. 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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