View source for 2iyw


==Shikimate kinase from Mycobacterium tuberculosis in complex with MgATP, open LID (conf. B)==
<StructureSection load='2iyw' size='340' side='right'caption='[[2iyw]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2iyw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IYW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l4u|1l4u]], [[1l4y|1l4y]], [[1u8a|1u8a]], [[1zyu|1zyu]], [[2g1j|2g1j]], [[2g1k|2g1k]], [[2iyq|2iyq]], [[2iyr|2iyr]], [[2iys|2iys]], [[2iyt|2iyt]], [[2iyu|2iyu]], [[2iyv|2iyv]], [[2iyx|2iyx]], [[2iyy|2iyy]], [[2iyz|2iyz]]</div></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=2iyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyw OCA], [https://pdbe.org/2iyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iyw RCSB], [https://www.ebi.ac.uk/pdbsum/2iyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyw 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/2iyw_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=2iyw 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2iyw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Shikimate kinase|Shikimate kinase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Myctu]]
[[Category: Shikimate kinase]]
[[Category: Bartunik, H D]]
[[Category: Bourenkov, G P]]
[[Category: Hartmann, M D]]
[[Category: Oberschall, A]]
[[Category: Strizhov, N]]
[[Category: Amino-acid biosynthesis]]
[[Category: Aromatic amino acid biosynthesis]]
[[Category: Atp-binding]]
[[Category: Kinase]]
[[Category: Magnesium]]
[[Category: Metal- binding]]
[[Category: Nucleotide- binding]]
[[Category: P-loop kinase]]
[[Category: Shikimate pathway]]
[[Category: Transferase]]