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2h0g
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2h0g.png|left|200px]] | ||
| - | < | + | ==Crystal Structure of DsbG T200M mutant== |
| - | + | <StructureSection load='2h0g' size='340' side='right'caption='[[2h0g]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2h0g]] 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=2H0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H0G FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | |
| - | + | <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'>[https://proteopedia.org/fgij/fg.htm?mol=2h0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h0g OCA], [https://pdbe.org/2h0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h0g RCSB], [https://www.ebi.ac.uk/pdbsum/2h0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h0g ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == 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> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/2h0g_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2h0g ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | |
| - | < | + | |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Bardwell | + | [[Category: Large Structures]] |
| - | [[Category: Heras | + | [[Category: Bardwell JCA]] |
| - | [[Category: Hiniker | + | [[Category: Heras B]] |
| - | [[Category: Martin | + | [[Category: Hiniker A]] |
| - | [[Category: Stuckey | + | [[Category: Martin JL]] |
| - | + | [[Category: Stuckey J]] | |
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Current revision
Crystal Structure of DsbG T200M mutant
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