3tdg: Difference between revisions

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 ==Structural and functional characterization of Helicobacter pylori DsbG==
-<StructureSection load='3tdg' size='340' side='right' caption='[[3tdg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='3tdg' size='340' side='right'caption='[[3tdg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tdg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TDG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tdg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TDG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</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]] 2.1&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0231 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdg OCA], [http://pdbe.org/3tdg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tdg RCSB], [http://www.ebi.ac.uk/pdbsum/3tdg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tdg 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=3tdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdg OCA], [https://pdbe.org/3tdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tdg RCSB], [https://www.ebi.ac.uk/pdbsum/3tdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tdg ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/O25017_HELPY O25017_HELPY]
-Dsb proteins play important roles in bacterial pathogenicity. To better understand the role of Dsb proteins in Helicobacter pylori, we have structurally and functionally characterized H. pylori DsbG (HP0231). The monomer consists of two domains connected by a helical linker. Two monomers associate to form a V-shaped dimer. The monomeric and dimeric structures of H. pylori DsbG show significant differences compared to Escherichia coli DsbG. Two polyethylene glycol molecules are bound in the cleft of the V-shaped dimer, suggesting a possible role as a chaperone. Furthermore, we show that H. pylori DsbG functions as a reductase against HP0518, a putative L,D-transpeptidase with a catalytic cysteine residue.
-Structural and functional characterization of Helicobacter pylori DsbG.,Yoon JY, Kim J, Lee SJ, Kim HS, Im HN, Yoon HJ, Kim KH, Kim SJ, Han BW, Suh SW FEBS Lett. 2011 Dec 15;585(24):3862-7. doi: 10.1016/j.febslet.2011.10.042. Epub, 2011 Nov 2. PMID:22062156<ref>PMID:22062156</ref>
+==See Also==
+*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3tdg" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 43504]]
+[[Category: Helicobacter pylori]]
-[[Category: Han, B W]]
+[[Category: Large Structures]]
-[[Category: Im, H N]]
+[[Category: Han BW]]
-[[Category: Kim, H S]]
+[[Category: Im HN]]
-[[Category: Kim, J]]
+[[Category: Kim HS]]
-[[Category: Kim, K H]]
+[[Category: Kim J]]
-[[Category: Kim, S]]
+[[Category: Kim KH]]
-[[Category: Lee, S J]]
+[[Category: Kim S]]
-[[Category: Suh, S W]]
+[[Category: Lee SJ]]
-[[Category: Yoon, H]]
+[[Category: Suh SW]]
-[[Category: Yoon, J Y]]
+[[Category: Yoon H]]
-[[Category: Oxidoreductase]]
+[[Category: Yoon JY]]
-[[Category: Reductase]]
-[[Category: Thioredoxin fold]]