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Title: Crystal structure of chorismate mutase from Burkholderia thailandensis

Abstract

Burkholderia thailandensisis 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 fromB. thailandensis, have been determined by the Seattle Structural Genomics Center for Infectious Disease. The high-resolution structure of chorismate mutase fromB. thailandensiswas determined in the monoclinic space groupP2 1with 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.

Authors:
ORCiD logo; ; ; ; ; ; ORCiD logo
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NIAIDNIH
OSTI Identifier:
1498431
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F, Structural Biology Communications
Additional Journal Information:
Journal Volume: 74; Journal Issue: 5; Journal ID: ISSN 2053-230X
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Asojo, Oluwatoyin A., Dranow, David M., Serbzhinskiy, Dmitry, Subramanian, Sandhya, Staker, Bart, Edwards, Thomas E., and Myler, Peter J. Crystal structure of chorismate mutase from Burkholderia thailandensis. United States: N. p., 2018. Web. doi:10.1107/S2053230X1800506X.
Asojo, Oluwatoyin A., Dranow, David M., Serbzhinskiy, Dmitry, Subramanian, Sandhya, Staker, Bart, Edwards, Thomas E., & Myler, Peter J. Crystal structure of chorismate mutase from Burkholderia thailandensis. United States. doi:10.1107/S2053230X1800506X.
Asojo, Oluwatoyin A., Dranow, David M., Serbzhinskiy, Dmitry, Subramanian, Sandhya, Staker, Bart, Edwards, Thomas E., and Myler, Peter J. Mon . "Crystal structure of chorismate mutase from Burkholderia thailandensis". United States. doi:10.1107/S2053230X1800506X.
@article{osti_1498431,
title = {Crystal structure of chorismate mutase from Burkholderia thailandensis},
author = {Asojo, Oluwatoyin A. and Dranow, David M. and Serbzhinskiy, Dmitry and Subramanian, Sandhya and Staker, Bart and Edwards, Thomas E. and Myler, Peter J.},
abstractNote = {Burkholderia thailandensisis 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 fromB. thailandensis, have been determined by the Seattle Structural Genomics Center for Infectious Disease. The high-resolution structure of chorismate mutase fromB. thailandensiswas determined in the monoclinic space groupP21with 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.},
doi = {10.1107/S2053230X1800506X},
journal = {Acta Crystallographica. Section F, Structural Biology Communications},
issn = {2053-230X},
number = 5,
volume = 74,
place = {United States},
year = {2018},
month = {4}
}

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