View source for 5ts9


==Crystal structure of Chorismate mutase from Burkholderia phymatum==
<StructureSection load='5ts9' size='340' side='right'caption='[[5ts9]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ts9]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Paraburkholderia_phymatum_STM815 Paraburkholderia phymatum STM815]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TS9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TS9 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]] 1.95&#8491;</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=5ts9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ts9 OCA], [https://pdbe.org/5ts9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ts9 RCSB], [https://www.ebi.ac.uk/pdbsum/5ts9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ts9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B2JYH9_PARP8 B2JYH9_PARP8] 
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== Publication Abstract from PubMed ==
The bacterium Burkholderia phymatum is a promiscuous symbiotic nitrogen-fixating bacterium that belongs to one of the largest groups of Betaproteobacteria. Other Burkholderia species are known to cause disease in plants and animals, and some are potential agents for biological warfare. Structural genomics efforts include characterizing the structures of enzymes from pathways that can be targeted for drug development. As part of these efforts, chorismate mutase from B. phymatum was produced and crystallized, and a 1.95 A resolution structure is reported. This enzyme shares less than 33% sequence identity with other homologs of known structure. There are two classes of chorismate mutase: AroQ and AroH. The bacterial subclass AroQgamma has reported roles in virulence. Chorismate mutase from B. phymatum has the prototypical AroQgamma topology and retains the characteristic chorismate mutase active site. This suggests that substrate-based chorismate mutase inhibitors will not be specific and are likely to affect beneficial bacteria such as B. phymatum.

Crystal structure of chorismate mutase from Burkholderia phymatum.,Asojo OA, Subramanian S, Abendroth J, Exley I, Lorimer DD, Edwards TE, Myler PJ Acta Crystallogr F Struct Biol Commun. 2018 Apr 1;74(Pt 4):187-192. doi:, 10.1107/S2053230X18002868. Epub 2018 Mar 22. PMID:29633965<ref>PMID:29633965</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5ts9" style="background-color:#fffaf0;"></div>

==See Also==
*[[3D structures of chorismate mutase|3D structures of chorismate mutase]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Paraburkholderia phymatum STM815]]