2vkl: Difference between revisions

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-{{Seed}}
-[[Image:2vkl.png|left|200px]]
-<!--
+==X-ray crystal structure of the intracellular Chorismate mutase from Mycobactrerium Tuberculosis in complex with malate==
-The line below this paragraph, containing "STRUCTURE_2vkl", creates the "Structure Box" on the page.
+<StructureSection load='2vkl' size='340' side='right'caption='[[2vkl]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2vkl]] 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=2VKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VKL FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr>
-{{STRUCTURE_2vkl|  PDB=2vkl  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkl OCA], [https://pdbe.org/2vkl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vkl RCSB], [https://www.ebi.ac.uk/pdbsum/2vkl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vkl ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHMU_MYCTU CHMU_MYCTU] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:15737998</ref> <ref>PMID:18727669</ref> <ref>PMID:19556970</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/vk/2vkl_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=2vkl ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Chorismate mutase catalyzes a key step in the shikimate biosynthetic pathway towards phenylalanine and tyrosine. Curiously, the intracellular chorismate mutase of Mycobacterium tuberculosis (MtCM; Rv0948c) has poor activity and lacks prominent active-site residues. However, its catalytic efficiency increases &gt;100-fold on addition of DAHP synthase (MtDS; Rv2178c), another shikimate-pathway enzyme. The 2.35 A crystal structure of the MtCM-MtDS complex bound to a transition-state analogue shows a central core formed by four MtDS subunits sandwiched between two MtCM dimers. Structural comparisons imply catalytic activation to be a consequence of the repositioning of MtCM active-site residues on binding to MtDS. The mutagenesis of the C-terminal extrusion of MtCM establishes conserved residues as part of the activation machinery. The chorismate-mutase activity of the complex, but not of MtCM alone, is inhibited synergistically by phenylalanine and tyrosine. The complex formation thus endows the shikimate pathway of M. tuberculosis with an important regulatory feature. Experimental evidence suggests that such non-covalent enzyme complexes comprising an AroQ(delta) subclass chorismate mutase like MtCM are abundant in the bacterial order Actinomycetales.
-===X-RAY CRYSTAL STRUCTURE OF THE INTRACELLULAR CHORISMATE MUTASE FROM MYCOBACTRERIUM TUBERCULOSIS IN COMPLEX WITH MALATE===
+Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner.,Sasso S, Okvist M, Roderer K, Gamper M, Codoni G, Krengel U, Kast P EMBO J. 2009 Jul 22;28(14):2128-42. Epub 2009 Jun 25. PMID:19556970<ref>PMID:19556970</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2vkl" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-VKL is a 1 chain structure of 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=2VKL OCA].
+*[[3D structures of chorismate mutase|3D structures of chorismate mutase]]
-[[Category: Chorismate mutase]]
+== References ==
-[[Category: Mycobacterium tuberculosis]]
+<references/>
-[[Category: Kast, P.]]
+__TOC__
-[[Category: Krengel, U.]]
+</StructureSection>
-[[Category: Okvist, M.]]
+[[Category: Large Structures]]
-[[Category: Roderer, K.]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Sasso, S.]]
+[[Category: Kast P]]
-[[Category: Chorismate mutase]]
+[[Category: Krengel U]]
-[[Category: Helical]]
+[[Category: Okvist M]]
-[[Category: Intracellular]]
+[[Category: Roderer K]]
-[[Category: Isomerase]]
+[[Category: Sasso S]]
-[[Category: Tuberculosis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 19 20:12:21 2009''