4oe7
From Proteopedia
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==Crystal structure of YagE, a KDG aldolase protein, in complex with aldol condensed product of pyruvate and glyoxal== | ==Crystal structure of YagE, a KDG aldolase protein, in complex with aldol condensed product of pyruvate and glyoxal== | ||
<StructureSection load='4oe7' size='340' side='right' caption='[[4oe7]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='4oe7' size='340' side='right' caption='[[4oe7]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GXP:(4S)-4-HYDROXY-2,5-DIOXOPENTANOIC+ACID'>GXP</scene>, <scene name='pdbligand=GXS:(4R)-4-HYDROXY-2,5-DIOXOPENTANOIC+ACID'>GXS</scene>, <scene name='pdbligand=GXT:ETHANEDIAL'>GXT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GXP:(4S)-4-HYDROXY-2,5-DIOXOPENTANOIC+ACID'>GXP</scene>, <scene name='pdbligand=GXS:(4R)-4-HYDROXY-2,5-DIOXOPENTANOIC+ACID'>GXS</scene>, <scene name='pdbligand=GXT:ETHANEDIAL'>GXT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v8z|2v8z]], [[3n2x|3n2x]], [[3nev|3nev]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v8z|2v8z]], [[3n2x|3n2x]], [[3nev|3nev]]</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=4oe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oe7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oe7 RCSB], [http://www.ebi.ac.uk/pdbsum/4oe7 PDBsum]</span></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=4oe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oe7 OCA], [http://pdbe.org/4oe7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oe7 RCSB], [http://www.ebi.ac.uk/pdbsum/4oe7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oe7 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/YAGE_ECOLI YAGE_ECOLI]] Catalyzes the formation of 2-keto-3-deoxy-galactonate (KDGal) from pyruvate and glyceraldehyde. Overexpression leads to increased growth (over 2 hours) in the presence of the antibiotics norfloxacin, ampicillin and streptomycin. | [[http://www.uniprot.org/uniprot/YAGE_ECOLI YAGE_ECOLI]] Catalyzes the formation of 2-keto-3-deoxy-galactonate (KDGal) from pyruvate and glyceraldehyde. Overexpression leads to increased growth (over 2 hours) in the presence of the antibiotics norfloxacin, ampicillin and streptomycin. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | YagE is a 33 kDa prophage protein encoded by CP4-6 prophage element in Escherichia coli K12 genome. Here, we report the structures of YagE complexes with pyruvate (PDB Id 3N2X) and KDGal (2-keto-3-deoxy galactonate) (PDB Id 3NEV) at 2.2A resolution. Pyruvate depletion assay in presence of glyceraldehyde shows that YagE catalyses the aldol condensation of pyruvate and glyceraldehyde. Our results indicate that the biochemical function of YagE is that of a 2-keto-3-deoxy gluconate (KDG) aldolase. Interestingly, E. coli K12 genome lacks an intrinsic KDG aldolase. Moreover, the over-expression of YagE increases cell viability in the presence of certain bactericidal antibiotics, indicating a putative biological role of YagE as a prophage encoded virulence factor enabling the survival of bacteria in the presence of certain antibiotics. The analysis implies a possible mechanism of antibiotic resistance conferred by the over-expression of prophage encoded YagE to E. coli. Proteins 2011, (c) 2011 Wiley-Liss, Inc. | ||
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| + | Identification of biochemical and putative biological role of a xenolog from Escherichia coli using structural analysis.,Bhaskar V, Kumar M, Manicka S, Tripathi S, Venkatraman A, Krishnaswamy S Proteins. 2011 Apr;79(4):1132-42. doi: 10.1002/prot.22949. Epub 2011 Feb, 3. PMID:21294156<ref>PMID:21294156</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4oe7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 16:43, 5 August 2016
Crystal structure of YagE, a KDG aldolase protein, in complex with aldol condensed product of pyruvate and glyoxal
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