5g1l: Difference between revisions
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<StructureSection load='5g1l' size='340' side='right'caption='[[5g1l]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5g1l' size='340' side='right'caption='[[5g1l]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5g1l]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5g1l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G1L FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5g1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1l OCA], [https://pdbe.org/5g1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g1l RCSB], [https://www.ebi.ac.uk/pdbsum/5g1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DSBG_ECOLI DSBG_ECOLI] Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro.<ref>PMID:19965429</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Boudier | [[Category: Boudier A]] | ||
[[Category: Collet | [[Category: Collet JF]] | ||
[[Category: Lafaye C]] | |||
[[Category: Lafaye | [[Category: Leroy P]] | ||
[[Category: Leroy | [[Category: Messens J]] | ||
[[Category: Messens | [[Category: Tamu Dufe V]] | ||
[[Category: | [[Category: Van Molle I]] | ||
[[Category: | [[Category: Wahni K]] | ||
[[Category: | |||