3d31: Difference between revisions

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<StructureSection load='3d31' size='340' side='right'caption='[[3d31]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3d31' size='340' side='right'caption='[[3d31]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[3d31]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans] and [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans_C2A Methanosarcina acetivorans C2A]. 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" id="ligandDat"><scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene></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]] 3&#8491;</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'>[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>
<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>
== Function ==
[https://www.uniprot.org/uniprot/Q8TTZ3_METAC Q8TTZ3_METAC]
== 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=3d31 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=3d31 ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transport 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<ref>PMID:18511655</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3d31" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Methanosarcina acetivorans]]
[[Category: Methanosarcina acetivorans]]
[[Category: Comellas-Bigler, M]]
[[Category: Methanosarcina acetivorans C2A]]
[[Category: Gerber, S]]
[[Category: Comellas-Bigler M]]
[[Category: Locher, K P]]
[[Category: Gerber S]]
[[Category: Atp-binding]]
[[Category: Locher KP]]
[[Category: Membrane]]
[[Category: Nucleotide-binding]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport protein]]

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