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Crystal structure of chorismate mutase from Burkholderia thailandensis
Author(s) -
Asojo Oluwatoyin A.,
Dranow David M.,
Serbzhinskiy Dmitry,
Subramanian Sandhya,
Staker Bart,
Edwards Thomas E.,
Myler Peter J.
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1800506x
Subject(s) - chorismate mutase , burkholderia , structural genomics , mutase , biology , microbiology and biotechnology , isomerase , protein structure , stereochemistry , chemistry , biochemistry , enzyme , bacteria , genetics , biosynthesis
Burkholderia 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 P 2 1 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQγ topology and shares conserved binding‐cavity residues with other chorismate mutases, including those with which it has no appreciable sequence identity.