1oxs
From Proteopedia
(New page: 200px<br /><applet load="1oxs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oxs, resolution 1.65Å" /> '''Crystal structure of...) |
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| - | [[Image:1oxs.jpg|left|200px]]<br /><applet load="1oxs" size=" | + | [[Image:1oxs.jpg|left|200px]]<br /><applet load="1oxs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oxs, resolution 1.65Å" /> | caption="1oxs, resolution 1.65Å" /> | ||
'''Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus'''<br /> | '''Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ABC-ATPase GlcV energizes a binding protein-dependent ABC transporter | + | 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== | ==About this Structure== | ||
| - | 1OXS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with IOD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1OXS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=IOD:'>IOD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
| - | [[Category: Albers, S | + | [[Category: Albers, S V.]] |
| - | [[Category: Dijkstra, B | + | [[Category: Dijkstra, B W.]] |
| - | [[Category: Driessen, A | + | [[Category: Driessen, A J.]] |
| - | [[Category: Thunnissen, A | + | [[Category: Thunnissen, A M.]] |
[[Category: Verdon, G.]] | [[Category: Verdon, G.]] | ||
[[Category: IOD]] | [[Category: IOD]] | ||
| Line 25: | Line 25: | ||
[[Category: sulfolobus solfataricus]] | [[Category: sulfolobus solfataricus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:53 2008'' |
Revision as of 12:22, 21 February 2008
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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
1OXS is a Single protein structure of sequence from Sulfolobus solfataricus with as ligand. 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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