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Title: Crystal structure of Staphylococcus aureus Zn-glyoxalase I: new subfamily of glyoxalase I family

Abstract

The crystal structures of protein SA0856 from Staphylococcus aureus in its apo-form and in complex with a Zn2+-ion have been presented. The 152 amino acid protein consists of two similar domains with α + β topology. In both crystalline state and in solution, the protein forms a dimer with monomers related by a twofold pseudo-symmetry rotation axis. A sequence homology search identified the protein as a member of the structural family Glyoxalase I. We have shown that the enzyme possesses glyoxalase I activity in the presence of Zn2+, Mg2+, Ni2+, and Co2+, in this order of preference. Sequence and structure comparisons revealed that human glyoxalase I should be assigned to a subfamily A, while S. aureus glyoxalase I represents a new subfamily B, which includes also proteins from other bacteria. Both subfamilies have a similar protein chain fold but rather diverse sequences. The active sites of human and staphylococcus glyoxalases I are also different: the former contains one Zn-ion per chain; the latter incorporates two of these ions. In the active site of SA0856, the first Zn-ion is well coordinated by His58, Glu60 from basic molecule and Glu40*, His44* from adjacent symmetry-related molecule. The second Zn3-ion is coordinated only bymore » residue His143 from protein molecule and one acetate ion. We suggest that only single Zn1-ion plays the role of catalytic center. The newly found differences between the two subfamilies could guide the design of new drugs against S. aureus, an important pathogenic micro-organism.« less

Authors:
 [1];  [1];  [2];  [3];  [4];  [4];  [4];  [5];  [6]
  1. Institute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Moscow Region, Russia
  2. Advanced Photon Source, Argonne National Laboratory, Hauptman–Woodward Medical Research Institute, IMCA-CAT, Argonne, IL 60439, USA
  3. Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK
  4. Campbell Family Cancer Research Institute, Ontario Cancer Institute, Princess Margaret Hospital, University Health Network, Toronto, Ontario M5G 2C4, Canada
  5. Campbell Family Cancer Research Institute, Ontario Cancer Institute, Princess Margaret Hospital, University Health Network, Toronto, Ontario M5G 2C4, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada; Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada; Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5S 1A8, Canada
  6. Campbell Family Cancer Research Institute, Ontario Cancer Institute, Princess Margaret Hospital, University Health Network, Toronto, Ontario M5G 2C4, Canada; Department of Pharmacology and Toxicology, University of Toronto, Toronto, Ontario M5S 1A8, Canada; X-CHIP Technologies Inc., Toronto, Ontario, Canada
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1418025
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Biomolecular Structure and Dynamics; Journal Volume: 36; Journal Issue: 2
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Chirgadze, Yuri N., Boshkova, Eugenia A., Battaile, Kevin P., Mendes, Vitor G., Lam, Robert, Chan, Tiffany S. Y., Romanov, Vladimir, Pai, Emil F., and Chirgadze, Nickolay Y. Crystal structure of Staphylococcus aureus Zn-glyoxalase I: new subfamily of glyoxalase I family. United States: N. p., 2017. Web. doi:10.1080/07391102.2016.1278038.
Chirgadze, Yuri N., Boshkova, Eugenia A., Battaile, Kevin P., Mendes, Vitor G., Lam, Robert, Chan, Tiffany S. Y., Romanov, Vladimir, Pai, Emil F., & Chirgadze, Nickolay Y. Crystal structure of Staphylococcus aureus Zn-glyoxalase I: new subfamily of glyoxalase I family. United States. doi:10.1080/07391102.2016.1278038.
Chirgadze, Yuri N., Boshkova, Eugenia A., Battaile, Kevin P., Mendes, Vitor G., Lam, Robert, Chan, Tiffany S. Y., Romanov, Vladimir, Pai, Emil F., and Chirgadze, Nickolay Y. Mon . "Crystal structure of Staphylococcus aureus Zn-glyoxalase I: new subfamily of glyoxalase I family". United States. doi:10.1080/07391102.2016.1278038.
@article{osti_1418025,
title = {Crystal structure of Staphylococcus aureus Zn-glyoxalase I: new subfamily of glyoxalase I family},
author = {Chirgadze, Yuri N. and Boshkova, Eugenia A. and Battaile, Kevin P. and Mendes, Vitor G. and Lam, Robert and Chan, Tiffany S. Y. and Romanov, Vladimir and Pai, Emil F. and Chirgadze, Nickolay Y.},
abstractNote = {The crystal structures of protein SA0856 from Staphylococcus aureus in its apo-form and in complex with a Zn2+-ion have been presented. The 152 amino acid protein consists of two similar domains with α + β topology. In both crystalline state and in solution, the protein forms a dimer with monomers related by a twofold pseudo-symmetry rotation axis. A sequence homology search identified the protein as a member of the structural family Glyoxalase I. We have shown that the enzyme possesses glyoxalase I activity in the presence of Zn2+, Mg2+, Ni2+, and Co2+, in this order of preference. Sequence and structure comparisons revealed that human glyoxalase I should be assigned to a subfamily A, while S. aureus glyoxalase I represents a new subfamily B, which includes also proteins from other bacteria. Both subfamilies have a similar protein chain fold but rather diverse sequences. The active sites of human and staphylococcus glyoxalases I are also different: the former contains one Zn-ion per chain; the latter incorporates two of these ions. In the active site of SA0856, the first Zn-ion is well coordinated by His58, Glu60 from basic molecule and Glu40*, His44* from adjacent symmetry-related molecule. The second Zn3-ion is coordinated only by residue His143 from protein molecule and one acetate ion. We suggest that only single Zn1-ion plays the role of catalytic center. The newly found differences between the two subfamilies could guide the design of new drugs against S. aureus, an important pathogenic micro-organism.},
doi = {10.1080/07391102.2016.1278038},
journal = {Journal of Biomolecular Structure and Dynamics},
number = 2,
volume = 36,
place = {United States},
year = {Mon Jan 16 00:00:00 EST 2017},
month = {Mon Jan 16 00:00:00 EST 2017}
}