1oxt: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='1oxt' size='340' side='right'caption='[[1oxt]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == 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>
+== 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]]
@@ Line 18: / Line 19: @@
 </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="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==
@@ Line 34: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 35091]]
 [[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]]