6cnz: Difference between revisions
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==Crystal Structure of Chorismate Mutase from Burkholderia thailandensis== | ==Crystal Structure of Chorismate Mutase from Burkholderia thailandensis== | ||
<StructureSection load='6cnz' size='340' side='right' caption='[[6cnz]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='6cnz' size='340' side='right'caption='[[6cnz]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6cnz]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6cnz]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_thailandensis Burkholderia thailandensis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4oj7 4oj7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CNZ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=6cnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cnz OCA], [https://pdbe.org/6cnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cnz RCSB], [https://www.ebi.ac.uk/pdbsum/6cnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cnz ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/A0A1B4JXW9_BURTH A0A1B4JXW9_BURTH] Catalyzes the Claisen rearrangement of chorismate to prephenate.[PIRNR:PIRNR026640] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6cnz" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6cnz" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[3D structures of chorismate mutase|3D structures of chorismate mutase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Burkholderia thailandensis]] | ||
[[Category: | [[Category: Large Structures]] | ||
Latest revision as of 18:08, 4 October 2023
Crystal Structure of Chorismate Mutase from Burkholderia thailandensisCrystal Structure of Chorismate Mutase from Burkholderia thailandensis
Structural highlights
FunctionA0A1B4JXW9_BURTH Catalyzes the Claisen rearrangement of chorismate to prephenate.[PIRNR:PIRNR026640] Publication Abstract from PubMedBurkholderia thailandensis is often used as a model for more virulent members of this genus of proteobacteria that are highly antibiotic-resistant and are potential agents of biological warfare that are infective by inhalation. As part of ongoing efforts to identify potential targets for the development of rational therapeutics, the structures of enzymes that are absent in humans, including that of chorismate mutase from B. thailandensis, have been determined by the Seattle Structural Genomics Center for Infectious Disease. The high-resolution structure of chorismate mutase from B. thailandensis was determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQgamma topology and shares conserved binding-cavity residues with other chorismate mutases, including those with which it has no appreciable sequence identity. Crystal structure of chorismate mutase from Burkholderia thailandensis.,Asojo OA, Dranow DM, Serbzhinskiy D, Subramanian S, Staker B, Edwards TE, Myler PJ Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):294-299. doi:, 10.1107/S2053230X1800506X. Epub 2018 Apr 16. PMID:29717997[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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