View source for 3muf


==Shikimate kinase from Helicobacter pylori in complex with shikimate-3-phosphate and ADP==
<StructureSection load='3muf' size='340' side='right'caption='[[3muf]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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='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>
== 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> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:22438938</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3muf" style="background-color:#fffaf0;"></div>

==See Also==
*[[Shikimate kinase 3D structures|Shikimate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori]]
[[Category: Large Structures]]
[[Category: Chen TJ]]
[[Category: Cheng WC]]
[[Category: Lin SC]]
[[Category: Wang WC]]