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| | <StructureSection load='4y0a' size='340' side='right'caption='[[4y0a]], [[Resolution|resolution]] 1.91Å' scene=''> | | <StructureSection load='4y0a' size='340' side='right'caption='[[4y0a]], [[Resolution|resolution]] 1.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y0a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acib3 Acib3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y0A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y0a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_AB307-0294 Acinetobacter baumannii AB307-0294]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y0A FirstGlance]. <br> |
| - | </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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.911Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aroK, ABBFA_000324 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=557600 ACIB3])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4y0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0a OCA], [https://pdbe.org/4y0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y0a RCSB], [https://www.ebi.ac.uk/pdbsum/4y0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0a ProSAT]</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0M3KL09_ACIB3 A0A0M3KL09_ACIB3] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.[HAMAP-Rule:MF_00109] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Shikimate kinase|Shikimate kinase]] | + | *[[Shikimate kinase 3D structures|Shikimate kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acib3]] | + | [[Category: Acinetobacter baumannii AB307-0294]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Shikimate kinase]]
| + | [[Category: Beanan JM]] |
| - | [[Category: Beanan, J M]] | + | [[Category: Breen J]] |
| - | [[Category: Breen, J]] | + | [[Category: MacDonald U]] |
| - | [[Category: MacDonald, U]] | + | [[Category: Olson R]] |
| - | [[Category: Olson, R]] | + | [[Category: Russo TA]] |
| - | [[Category: Russo, T A]] | + | [[Category: Schultz LW]] |
| - | [[Category: Schultz, L W]] | + | [[Category: Sutton KA]] |
| - | [[Category: Sutton, K A]] | + | [[Category: Umland TC]] |
| - | [[Category: Umland, T C]] | + | |
| - | [[Category: Amino acid biosynthesis]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Nucleotide binding]]
| + | |
| - | [[Category: Shikimate pathway]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase-transferase inhibitor complex]]
| + | |
| Structural highlights
Function
A0A0M3KL09_ACIB3 Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.[HAMAP-Rule:MF_00109]
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sutton KA, Breen J, MacDonald U, Beanan JM, Olson R, Russo TA, Schultz LW, Umland TC. Structure of shikimate kinase, an in vivo essential metabolic enzyme in the nosocomial pathogen Acinetobacter baumannii, in complex with shikimate. Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1736-44. doi:, 10.1107/S139900471501189X. Epub 2015 Jul 31. PMID:26249354 doi:http://dx.doi.org/10.1107/S139900471501189X
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