4xo1
From Proteopedia
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| - | ''' | + | ==crystal structure of Se-Met GnsA with double mutations== |
| + | <StructureSection load='4xo1' size='340' side='right' caption='[[4xo1]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xo1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XO1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xo2|4xo2]]</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=4xo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xo1 RCSB], [http://www.ebi.ac.uk/pdbsum/4xo1 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GNSA_ECOLI GNSA_ECOLI]] Overexpression increases levels of unsaturated fatty acids and suppresses both the temperature-sensitive fabA6 mutation and cold-sensitive secG null mutation.<ref>PMID:11544213</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Escherichia Coli GnsA is a regulator of phosphatidylethanolamine synthesis and functions as a suppressor of both a secG null mutation and fabA6 mutations. GnsA may also be a toxin with the cognate antitoxin YmcE. Here we report the crystal structure of GnsA to 1.8 A. GnsA forms a V shaped hairpin structure that is tightly associated into a homodimer. Our comprehensive structural study suggests that GnsA is structurally similar to an outer membrane protein, suggesting a function of protein binding. | ||
| - | + | Crystal structure of GnsA from Escherichia coli.,Wei Y, Zhan L, Gao Z, Prive GG, Dong Y Biochem Biophys Res Commun. 2015 Jun 19;462(1):1-7. doi:, 10.1016/j.bbrc.2015.03.133. Epub 2015 Apr 1. PMID:25839658<ref>PMID:25839658</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Gao, Z | + | __TOC__ |
| - | [[Category: Zhan, L | + | </StructureSection> |
| - | [[Category: | + | [[Category: Dong, Y]] |
| + | [[Category: Gao, Z]] | ||
| + | [[Category: Zhan, L]] | ||
| + | [[Category: Protein binding]] | ||
| + | [[Category: Suppressor]] | ||
Revision as of 14:41, 29 July 2015
crystal structure of Se-Met GnsA with double mutations
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Categories: Dong, Y | Gao, Z | Zhan, L | Protein binding | Suppressor
