4y0a
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>SKM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>SKM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71] </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=4y0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y0a RCSB], [http://www.ebi.ac.uk/pdbsum/4y0a 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=4y0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0a OCA], [http://pdbe.org/4y0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y0a RCSB], [http://www.ebi.ac.uk/pdbsum/4y0a PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Acinetobacter baumannii is an opportunistic Gram-negative pathogen that is an important cause of healthcare-associated infections exhibiting high mortality rates. Clinical isolates of multidrug-resistant (MDR) and extremely drug-resistant (XDR) A. baumannii strains are increasingly being observed. Compounding this concern is the dearth of new antibacterial agents in late-stage development that are effective against MDR and XDR A. baumannii. As part of an effort to address these concerns, two genes (aroA and aroC) of the shikimate pathway have previously been determined to be essential for the growth and survival of A. baumannii during host infection (i.e. to be essential in vivo). This study expands upon these results by demonstrating that the A. baumannii aroK gene, encoding shikimate kinase (SK), is also essential in vivo in a rat soft-tissue infection model. The crystal structure of A. baumannii SK in complex with the substrate shikimate and a sulfate ion that mimics the binding interactions expected for the beta-phosphate of ATP was then determined to 1.91 A resolution and the enzyme kinetics were characterized. The flexible shikimate-binding domain and LID region are compared with the analogous regions in other SK crystal structures. The impact of structural differences and sequence divergence between SKs from pathogenic bacteria that may influence antibiotic-development efforts is discussed. | ||
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| + | Structure of shikimate kinase, an in vivo essential metabolic enzyme in the nosocomial pathogen Acinetobacter baumannii, in complex with shikimate.,Sutton KA, Breen J, MacDonald U, Beanan JM, Olson R, Russo TA, Schultz LW, Umland TC Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1736-44. doi:, 10.1107/S139900471501189X. Epub 2015 Jul 31. PMID:26249354<ref>PMID:26249354</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4y0a" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Shikimate kinase]] | [[Category: Shikimate kinase]] | ||
| + | [[Category: Beanan, J M]] | ||
| + | [[Category: Breen, J]] | ||
| + | [[Category: MacDonald, U]] | ||
| + | [[Category: Olson, R]] | ||
| + | [[Category: Russo, T A]] | ||
| + | [[Category: Schultz, L W]] | ||
[[Category: Sutton, K A]] | [[Category: Sutton, K A]] | ||
| + | [[Category: Umland, T C]] | ||
[[Category: Amino acid biosynthesis]] | [[Category: Amino acid biosynthesis]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
Revision as of 07:43, 7 October 2015
Shikimate kinase from Acinetobacter baumannii in complex with shikimate
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