2iyz
From Proteopedia
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| - | [[Image:2iyz.png|left|200px]]  | ||
| - | + | ==Shikimate kinase from Mycobacterium tuberculosis in complex with shikimate-3-phosphate and ADP==  | |
| + | <StructureSection load='2iyz' size='340' side='right'caption='[[2iyz]], [[Resolution|resolution]] 2.30Å' scene=''>  | ||
| + | == Structural highlights ==  | ||
| + | <table><tr><td colspan='2'>[[2iyz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IYZ 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]] 2.3Å</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=2iyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyz OCA], [https://pdbe.org/2iyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iyz RCSB], [https://www.ebi.ac.uk/pdbsum/2iyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyz ProSAT]</span></td></tr>  | ||
| + | </table>  | ||
| + | == Function ==  | ||
| + | [https://www.uniprot.org/uniprot/AROK_MYCTU AROK_MYCTU] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.<ref>PMID:11483005</ref> <ref>PMID:17020768</ref>   | ||
| + | == Evolutionary Conservation ==  | ||
| + | [[Image:Consurf_key_small.gif|200px|right]]  | ||
| + | Check<jmol>  | ||
| + |   <jmolCheckbox>  | ||
| + |     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/2iyz_consurf.spt"</scriptWhenChecked>  | ||
| + |     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>  | ||
| + |     <text>to colour the structure by Evolutionary Conservation</text>  | ||
| + |   </jmolCheckbox>  | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2iyz ConSurf].  | ||
| + | <div style="clear:both"></div>  | ||
| + | <div style="background-color:#fffaf0;">  | ||
| + | == Publication Abstract from PubMed ==  | ||
| + | The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment. Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate.  | ||
| - | + | Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis.,Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD J Mol Biol. 2006 Dec 1;364(3):411-23. Epub 2006 Sep 5. PMID:17020768<ref>PMID:17020768</ref>  | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>  | |
| + | </div>  | ||
| + | <div class="pdbe-citations 2iyz" style="background-color:#fffaf0;"></div>  | ||
| - | ==  | + | ==See Also==  | 
| - | [[  | + | *[[Shikimate kinase 3D structures|Shikimate kinase 3D structures]]  | 
| - | + | == References ==  | |
| - | ==  | + | <references/>  | 
| - | <  | + | __TOC__  | 
| - | [[Category:   | + | </StructureSection>  | 
| - | [[Category:   | + | [[Category: Large Structures]]  | 
| - | [[Category: Bartunik  | + | [[Category: Mycobacterium tuberculosis H37Rv]]  | 
| - | [[Category: Bourenkov  | + | [[Category: Bartunik HD]]  | 
| - | [[Category: Hartmann  | + | [[Category: Bourenkov GP]]  | 
| - | [[Category: Oberschall  | + | [[Category: Hartmann MD]]  | 
| - | [[Category: Strizhov  | + | [[Category: Oberschall A]]  | 
| - | + | [[Category: Strizhov N]]  | |
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Current revision
Shikimate kinase from Mycobacterium tuberculosis in complex with shikimate-3-phosphate and ADP
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