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| | <StructureSection load='3muf' size='340' side='right'caption='[[3muf]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3muf' size='340' side='right'caption='[[3muf]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3muf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MUF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3muf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MUF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=S3P:SHIKIMATE-3-PHOSPHATE'>S3P</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zuh|1zuh]], [[1zui|1zui]], [[3hr7|3hr7]], [[3mrs|3mrs]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=S3P:SHIKIMATE-3-PHOSPHATE'>S3P</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AROK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [https://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=3muf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3muf OCA], [https://pdbe.org/3muf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3muf RCSB], [https://www.ebi.ac.uk/pdbsum/3muf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3muf 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=3muf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3muf OCA], [https://pdbe.org/3muf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3muf RCSB], [https://www.ebi.ac.uk/pdbsum/3muf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3muf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/AROK_HELPY AROK_HELPY]] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.<ref>PMID:16291688</ref>
| + | [https://www.uniprot.org/uniprot/AROK_HELPY AROK_HELPY] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.<ref>PMID:16291688</ref> |
| | <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: Atcc 43504]] | + | [[Category: Helicobacter pylori]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Shikimate kinase]]
| + | [[Category: Chen TJ]] |
| - | [[Category: Chen, T J]] | + | [[Category: Cheng WC]] |
| - | [[Category: Cheng, W C]] | + | [[Category: Lin SC]] |
| - | [[Category: Lin, S C]] | + | [[Category: Wang WC]] |
| - | [[Category: Wang, W C]] | + | |
| - | [[Category: Helix-sheet complex]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
AROK_HELPY Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.[1]
Publication Abstract from PubMed
Shikimate kinase (SK), which catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid in the presence of ATP, is the enzyme in the fifth step of the shikimate pathway for biosynthesis of aromatic amino acids. This pathway is present in bacteria, fungi, and plants but absent in mammals and therefore represents an attractive target pathway for the development of new antimicrobial agents, herbicides, and antiparasitic agents. Here we investigated the detailed structure-activity relationship of SK from Helicobacter pylori (HpSK). Site-directed mutagenesis and isothermal titration calorimetry studies revealed critical conserved residues (D33, F48, R57, R116, and R132) that interact with shikimate and are therefore involved in catalysis. Crystal structures of HpSK.SO(4), R57A, and HpSK*shikimate-3-phosphate * ADP show a characteristic three-layer architecture and a conformationally elastic region consisting of F48, R57, R116, and R132, occupied by shikimate. The structure of the inhibitor complex, E114A * 162535, was also determined, which revealed a dramatic shift in the elastic LID region and resulted in conformational locking into a distinctive form. These results reveal considerable insight into the active-site chemistry of SKs and a selective inhibitor-induced-fit mechanism.
Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism.,Cheng WC, Chen YF, Wang HJ, Hsu KC, Lin SC, Chen TJ, Yang JM, Wang WC PLoS One. 2012;7(3):e33481. Epub 2012 Mar 16. PMID:22438938[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cheng WC, Chang YN, Wang WC. Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase. J Bacteriol. 2005 Dec;187(23):8156-63. PMID:16291688 doi:187/23/8156
- ↑ Cheng WC, Chen YF, Wang HJ, Hsu KC, Lin SC, Chen TJ, Yang JM, Wang WC. Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism. PLoS One. 2012;7(3):e33481. Epub 2012 Mar 16. PMID:22438938 doi:10.1371/journal.pone.0033481
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