Crystal structure of chorismate mutase from Burkholderia thailandensis

Abstract

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 P2 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.

Crystal structure of a short-chain dehydrogenase/reductase from Burkholderia phymatum in complex with NAD

“…This structure is part of structural genomics efforts at the Seattle Structural Genomics Center for Infectious Disease (Raymond et al, 2011;Myler et al, 2009;Baugh et al, 2013). This manuscript was completed in a partnership between Hampton University and the SSGCID (Asojo, Dranow et al, 2018;.…”