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- | [[Image:1oxu.jpg|left|200px]]<br /><applet load="1oxu" size="350" color="white" frame="true" align="right" spinBox="true" | |
- | caption="1oxu, resolution 2.10Å" /> | |
- | '''Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus'''<br /> | |
| | | |
- | ==Overview== | + | ==Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus== |
- | 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.
| + | <StructureSection load='1oxu' size='340' side='right'caption='[[1oxu]], [[Resolution|resolution]] 2.10Å' scene=''> |
| + | == Structural highlights == |
| + | <table><tr><td colspan='2'>[[1oxu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OXU FirstGlance]. <br> |
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxu OCA], [https://pdbe.org/1oxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxu RCSB], [https://www.ebi.ac.uk/pdbsum/1oxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxu ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/GLCV_SACS2 GLCV_SACS2] Part of the ABC transporter complex GlcSTUV involved in glucose uptake (Probable). Responsible for energy coupling to the transport system (PubMed:12823973, PubMed:14607117). In vitro, as a free subunit, exhibits a constitutive ATPase activity (PubMed:11807278).<ref>PMID:11807278</ref> <ref>PMID:12823973</ref> <ref>PMID:14607117</ref> <ref>PMID:10400586</ref> <ref>PMID:11260467</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/1oxu_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oxu ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | ==About this Structure== | + | ==See Also== |
- | 1OXU 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=MG:'>MG</scene>, <scene name='pdbligand=IOD:'>IOD</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXU OCA].
| + | *[[ABC transporter 3D structures|ABC transporter 3D structures]] |
- | | + | == References == |
- | ==Reference==
| + | <references/> |
- | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12823973 12823973]
| + | __TOC__ |
- | [[Category: Single protein]] | + | </StructureSection> |
- | [[Category: Sulfolobus solfataricus]] | + | [[Category: Large Structures]] |
- | [[Category: Albers, S V.]] | + | [[Category: Saccharolobus solfataricus]] |
- | [[Category: Dijkstra, B W.]] | + | [[Category: Albers SV]] |
- | [[Category: Driessen, A J.]] | + | [[Category: Dijkstra BW]] |
- | [[Category: Thunnissen, A M.]] | + | [[Category: Driessen AJ]] |
- | [[Category: Verdon, G.]] | + | [[Category: Thunnissen AM]] |
- | [[Category: ADP]]
| + | [[Category: Verdon G]] |
- | [[Category: IOD]]
| + | |
- | [[Category: MG]]
| + | |
- | [[Category: abc-atpase]]
| + | |
- | [[Category: atp-binding cassette]]
| + | |
- | [[Category: atpase]]
| + | |
- | [[Category: glcv]]
| + | |
- | [[Category: sulfolobus solfataricus]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:53 2008''
| + | |
| Structural highlights
Function
GLCV_SACS2 Part of the ABC transporter complex GlcSTUV involved in glucose uptake (Probable). Responsible for energy coupling to the transport system (PubMed:12823973, PubMed:14607117). In vitro, as a free subunit, exhibits a constitutive ATPase activity (PubMed:11807278).[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM. Purification, crystallization and preliminary X-ray diffraction analysis of an archaeal ABC-ATPase. Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):362-5. PMID:11807278 doi:10.1107/s0907444901020765
- ↑ Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM. Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations. J Mol Biol. 2003 Jul 4;330(2):343-58. PMID:12823973
- ↑ Verdon G, Albers SV, van Oosterwijk N, Dijkstra BW, Driessen AJ, Thunnissen AM. Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus. J Mol Biol. 2003 Nov 21;334(2):255-67. PMID:14607117
- ↑ Albers SV, Elferink MG, Charlebois RL, Sensen CW, Driessen AJ, Konings WN. Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein. J Bacteriol. 1999 Jul;181(14):4285-91. PMID:10400586 doi:10.1128/JB.181.14.4285-4291.1999
- ↑ Elferink MG, Albers SV, Konings WN, Driessen AJ. Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol Microbiol. 2001 Mar;39(6):1494-503. PMID:11260467 doi:10.1046/j.1365-2958.2001.02336.x
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