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| | ==The structure of BdcA (YjgI) from E. coli== | | ==The structure of BdcA (YjgI) from E. coli== |
| - | <StructureSection load='4pcv' size='340' side='right' caption='[[4pcv]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='4pcv' size='340' side='right'caption='[[4pcv]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pcv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_p0299438.9 Escherichia coli p0299438.9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PCV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PCV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pcv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_P0299438.9 Escherichia coli P0299438.9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PCV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2.05Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECP02994389_4551 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1116044 Escherichia coli P0299438.9])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=4pcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pcv OCA], [http://pdbe.org/4pcv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pcv RCSB], [http://www.ebi.ac.uk/pdbsum/4pcv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pcv 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=4pcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pcv OCA], [https://pdbe.org/4pcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pcv RCSB], [https://www.ebi.ac.uk/pdbsum/4pcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pcv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0J9X1Z4_ECOLX A0A0J9X1Z4_ECOLX] |
| | <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: Escherichia coli p0299438 9]] | + | [[Category: Escherichia coli P0299438 9]] |
| - | [[Category: Lord, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Page, R]] | + | [[Category: Lord D]] |
| - | [[Category: Peti, W]] | + | [[Category: Page R]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Peti W]] |
| Structural highlights
Function
A0A0J9X1Z4_ECOLX
Publication Abstract from PubMed
The Escherichia coli protein BdcA (previously referred to as YjgI) plays a key role in the dispersal of cells from bacterial biofilms, and its constitutive activation provides an attractive therapeutic target for dismantling these communities. In order to investigate the function of BdcA at a molecular level, we integrated structural and functional studies. Our 2.05 A structure of BdcA shows that it is a member of the NAD(P)(H)-dependent short-chain dehydrogenase/reductase (SDR) superfamily. Structural comparisons with other members of the SDR family suggested that BdcA binds NADP(H). This was demonstrated experimentally using thermal denaturation studies, which showed that BcdA binds specifically to NADPH. Subsequent ITC experiments further confirmed this result and reported a Kd of 25.9 microM. Thus, BdcA represents the newest member of the limited number of oxidoreductases shown to be involved in quorum sensing and biofilm dispersal.
BdcA, a protein important for Escherichia coli biofilm dispersal, is a short-chain dehydrogenase/reductase that binds specifically to NADPH.,Lord DM, Baran AU, Wood TK, Peti W, Page R PLoS One. 2014 Sep 22;9(9):e105751. doi: 10.1371/journal.pone.0105751., eCollection 2014. PMID:25244619[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lord DM, Baran AU, Wood TK, Peti W, Page R. BdcA, a protein important for Escherichia coli biofilm dispersal, is a short-chain dehydrogenase/reductase that binds specifically to NADPH. PLoS One. 2014 Sep 22;9(9):e105751. doi: 10.1371/journal.pone.0105751., eCollection 2014. PMID:25244619 doi:http://dx.doi.org/10.1371/journal.pone.0105751
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