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Title: An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Abstract

Burkholderia pseudomallei is a soil-dwelling bacterium endemic to Southeast Asia and Northern Australia. Burkholderia is responsible for melioidosis, a serious infection of the skin. The enzyme 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (PGAM) catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate, a key step in the glycolytic pathway. As such it is an extensively studied enzyme and X-ray crystal structures of PGAM enzymes from multiple species have been elucidated. Vanadate is a phosphate mimic that is a powerful tool for studying enzymatic mechanisms in phosphoryl-transfer enzymes such as phosphoglycerate mutase. However, to date no X-ray crystal structures of phosphoglycerate mutase have been solved with vanadate acting as a substrate mimic. Here, two vanadate complexes together with an ensemble of substrate and fragment-bound structures that provide a comprehensive picture of the function of the Burkholderia enzyme are reported.

Authors:
; ; ; ; ; ; ; ; ; ;  [1]
  1. UWASH
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NIHNIAID
OSTI Identifier:
1027142
Resource Type:
Journal Article
Journal Name:
Acta Crystallogr. F
Additional Journal Information:
Journal Volume: 67; Journal Issue: (9) ; 09, 2011; Journal ID: ISSN 1744-3091
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; CRYSTAL STRUCTURE; ENZYMES; PHOSPHATES; SUBSTRATES; VANADATES

Citation Formats

Davies, Douglas R, Staker, Bart L, Abendroth, Jan A, Edwards, Thomas E, Hartley, Robert, Leonard, Jess, Kim, Hidong, Rychel, Amanda L, Hewitt, Stephen N, Myler, Peter J, Stewart, Lance J, and Emerald). An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. United States: N. p., 2011. Web. doi:10.1107/S1744309111030405.
Davies, Douglas R, Staker, Bart L, Abendroth, Jan A, Edwards, Thomas E, Hartley, Robert, Leonard, Jess, Kim, Hidong, Rychel, Amanda L, Hewitt, Stephen N, Myler, Peter J, Stewart, Lance J, & Emerald). An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. United States. doi:10.1107/S1744309111030405.
Davies, Douglas R, Staker, Bart L, Abendroth, Jan A, Edwards, Thomas E, Hartley, Robert, Leonard, Jess, Kim, Hidong, Rychel, Amanda L, Hewitt, Stephen N, Myler, Peter J, Stewart, Lance J, and Emerald). Wed . "An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase". United States. doi:10.1107/S1744309111030405.
@article{osti_1027142,
title = {An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase},
author = {Davies, Douglas R and Staker, Bart L and Abendroth, Jan A and Edwards, Thomas E and Hartley, Robert and Leonard, Jess and Kim, Hidong and Rychel, Amanda L and Hewitt, Stephen N and Myler, Peter J and Stewart, Lance J and Emerald)},
abstractNote = {Burkholderia pseudomallei is a soil-dwelling bacterium endemic to Southeast Asia and Northern Australia. Burkholderia is responsible for melioidosis, a serious infection of the skin. The enzyme 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (PGAM) catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate, a key step in the glycolytic pathway. As such it is an extensively studied enzyme and X-ray crystal structures of PGAM enzymes from multiple species have been elucidated. Vanadate is a phosphate mimic that is a powerful tool for studying enzymatic mechanisms in phosphoryl-transfer enzymes such as phosphoglycerate mutase. However, to date no X-ray crystal structures of phosphoglycerate mutase have been solved with vanadate acting as a substrate mimic. Here, two vanadate complexes together with an ensemble of substrate and fragment-bound structures that provide a comprehensive picture of the function of the Burkholderia enzyme are reported.},
doi = {10.1107/S1744309111030405},
journal = {Acta Crystallogr. F},
issn = {1744-3091},
number = (9) ; 09, 2011,
volume = 67,
place = {United States},
year = {2011},
month = {12}
}