1oxt: Difference between revisions

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<StructureSection load='1oxt' size='340' side='right'caption='[[1oxt]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1oxt' size='340' side='right'caption='[[1oxt]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1oxt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OXT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1oxt]] 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=1OXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OXT FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1oxs|1oxs]], [[1oxu|1oxu]], [[1oxv|1oxv]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glcV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</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=1oxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxt OCA], [https://pdbe.org/1oxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxt RCSB], [https://www.ebi.ac.uk/pdbsum/1oxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxt ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1oxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxt OCA], [http://pdbe.org/1oxt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oxt RCSB], [http://www.ebi.ac.uk/pdbsum/1oxt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxt ProSAT]</span></td></tr>
</table>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1oxt ConSurf].
</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=1oxt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:12823973</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1oxt" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35091]]
[[Category: Large Structures]]
[[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: Abc-atpase]]
[[Category: Verdon G]]
[[Category: Atp-binding cassette]]
[[Category: Atpase]]
[[Category: Glcv]]
[[Category: Sulfolobus solfataricus]]
[[Category: Transport protein]]

Latest revision as of 11:03, 14 February 2024

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

Structural highlights

1oxt is a 3 chain structure with sequence from Saccharolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

1oxt, resolution 2.10Å

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