6cnz
Crystal Structure of Chorismate Mutase from Burkholderia thailandensisCrystal Structure of Chorismate Mutase from Burkholderia thailandensis
Structural highlights
Function[A0A1B4JXW9_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. References
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