2iyt: Difference between revisions

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-[[Image:2iyt.png|left|200px]]
-{{STRUCTURE_2iyt|  PDB=2iyt  |  SCENE=  }}
+==Shikimate kinase from Mycobacterium tuberculosis in unliganded state, open LID (conf. A)==
+<StructureSection load='2iyt' size='340' side='right'caption='[[2iyt]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2iyt]] 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=2IYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IYT 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]] 1.47&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=2iyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyt OCA], [https://pdbe.org/2iyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iyt RCSB], [https://www.ebi.ac.uk/pdbsum/2iyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyt 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/2iyt_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=2iyt 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.
-===SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN UNLIGANDED STATE, OPEN LID (CONF. A)===
+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>
-{{ABSTRACT_PUBMED_17020768}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2iyt" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[2iyt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYT OCA].
+*[[Shikimate kinase 3D structures|Shikimate kinase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:017020768</ref><references group="xtra"/>
+__TOC__
-[[Category: Mycobacterium tuberculosis]]
+</StructureSection>
-[[Category: Shikimate kinase]]
+[[Category: Large Structures]]
-[[Category: Bartunik, H D.]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Bourenkov, G P.]]
+[[Category: Bartunik HD]]
-[[Category: Hartmann, M D.]]
+[[Category: Bourenkov GP]]
-[[Category: Oberschall, A.]]
+[[Category: Hartmann MD]]
-[[Category: Strizhov, N.]]
+[[Category: Oberschall A]]
-[[Category: Amino-acid biosynthesis]]
+[[Category: Strizhov N]]
-[[Category: Aromatic amino acid biosynthesis]]
-[[Category: Atp-binding]]
-[[Category: Kinase]]
-[[Category: Magnesium]]
-[[Category: Metal- binding]]
-[[Category: Nucleotide- binding]]
-[[Category: P-loop kinase]]
-[[Category: Shikimate kinase]]
-[[Category: Shikimate pathway]]
-[[Category: Transferase]]