3d31: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==ModBC from Methanosarcina acetivorans== | ==ModBC from Methanosarcina acetivorans== | ||
<StructureSection load='3d31' size='340' side='right' caption='[[3d31]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='3d31' size='340' side='right'caption='[[3d31]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3d31]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3d31]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D31 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d31 OCA], [https://pdbe.org/3d31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d31 RCSB], [https://www.ebi.ac.uk/pdbsum/3d31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d31 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 28: | Line 28: | ||
==See Also== | ==See Also== | ||
*[[ABC transporter|ABC transporter]] | *[[ABC transporter 3D structures|ABC transporter 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Methanosarcina acetivorans]] | [[Category: Methanosarcina acetivorans]] | ||
[[Category: Comellas-Bigler, M]] | [[Category: Comellas-Bigler, M]] | ||
Revision as of 10:52, 2 February 2022
ModBC from Methanosarcina acetivoransModBC from Methanosarcina acetivorans
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTransport across cellular membranes is an essential process that is catalyzed by diverse membrane transport proteins. The turnover rates of certain transporters are inhibited by their substrates in a process termed trans-inhibition, whose structural basis is poorly understood. Here we present the crystal structure of a molybdate/tungstate ABC transporter (ModBC) from Methanosarcina acetivorans in a trans-inhibited state. The regulatory domains of the nucleotide-binding subunits are in close contact and provide two oxyanion binding pockets at the shared interface. By specifically binding to these pockets, molybdate or tungstate prevent ATPase activity and lock the transporter in an inward-facing conformation, with the catalytic motifs of the nucleotide-binding domains separated. This allosteric effect prevents the transporter from switching between the inward-facing and the outward-facing states, thus interfering with the alternating access and release mechanism. Structural Basis of Trans-Inhibition in a Molybdate/tungstate ABC Transporter.,Gerber S, Comellas-Bigler M, Goetz BA, Locher KP Science. 2008 May 29;. PMID:18511655[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||