3cw0

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Current revision (09:38, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3cw0' size='340' side='right'caption='[[3cw0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3cw0' size='340' side='right'caption='[[3cw0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3cw0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CW0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3cw0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CW0 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dmsD, ynfI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=3cw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cw0 OCA], [https://pdbe.org/3cw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cw0 RCSB], [https://www.ebi.ac.uk/pdbsum/3cw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cw0 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=3cw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cw0 OCA], [https://pdbe.org/3cw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cw0 RCSB], [https://www.ebi.ac.uk/pdbsum/3cw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cw0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DMSD_ECOLI DMSD_ECOLI]] Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein.<ref>PMID:11309116</ref> <ref>PMID:12527378</ref> <ref>PMID:12813051</ref> <ref>PMID:20153451</ref>
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[https://www.uniprot.org/uniprot/DMSD_ECOLI DMSD_ECOLI] Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein.<ref>PMID:11309116</ref> <ref>PMID:12527378</ref> <ref>PMID:12813051</ref> <ref>PMID:20153451</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=3cw0 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=3cw0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The translocation of folded proteins via the twin-arginine translocation (Tat) pathway is regulated to prevent the futile export of inactive substrate. DmsD is part of a class of cytoplasmic chaperones that play a role in preventing certain redox proteins from premature transport. DmsD from Escherichia coli has been crystallized in space group P4(1)2(1)2, with unit-cell parameters a = b = 97.45, c = 210.04 A, in the presence of a small peptide. The structure has been solved by molecular replacement to a resolution of 2.4 A and refined to an R factor of 19.4%. There are four molecules in the asymmetric unit that may mimic a higher order structure in vivo. There appears to be density for the peptide in a predicted binding pocket, which lends support to its role as the signal-recognition surface for this class of proteins.
 
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Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli.,Ramasamy SK, Clemons WM Jr Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Aug 1;65(Pt, 8):746-50. Epub 2009 Jul 21. PMID:19652330<ref>PMID:19652330</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3cw0" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Clemons, W]]
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[[Category: Clemons W]]
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[[Category: Ramasamy, S]]
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[[Category: Ramasamy S]]
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[[Category: Alpha-helice]]
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[[Category: Chaperone]]
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[[Category: Dmsd]]
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[[Category: Membrane]]
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Current revision

E.coli DmsD

PDB ID 3cw0

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