Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine

Alexander B. Taylor, David M. Benglis, Subramanian Dhandayuthapani, P. John Hart

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Peptide methionine sulfoxide reductase (MsrA) repairs oxidative damage to methionine residues arising from reactive oxygen species and reactive nitrogen intermediates. MsrA activity is found in a wide variety of organisms, and it is implicated as one of the primary defenses against oxidative stress. Disruption of the gene encoding MsrA in several pathogenic bacteria responsible for infections in humans results in the loss of their ability to colonize host cells. Here, we present the X-ray crystal structure of MsrA from the pathogenic bacterium Mycobacterium tuberculosis refined to 1.5 Å resolution. In contrast to the three catalytic cysteine residues found in previously characterized MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. The structure reveals a methionine residue of one MsrA molecule bound at the active site of a neighboring molecule in the crystal lattice and thus serves as an excellent model for protein-bound methionine sulfoxide recognition and repair.

Original languageEnglish (US)
Pages (from-to)4119-4126
Number of pages8
JournalJournal of Bacteriology
Volume185
Issue number14
DOIs
StatePublished - Jul 2003

Fingerprint

Methionine Sulfoxide Reductases
Mycobacterium tuberculosis
Methionine
Proteins
Cysteine
Bacteria
methionine sulfoxide reductase
Reactive Oxygen Species
Catalytic Domain
Oxidative Stress
Nitrogen
X-Rays

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine. / Taylor, Alexander B.; Benglis, David M.; Dhandayuthapani, Subramanian; Hart, P. John.

In: Journal of Bacteriology, Vol. 185, No. 14, 07.2003, p. 4119-4126.

Research output: Contribution to journalArticle

Taylor, Alexander B. ; Benglis, David M. ; Dhandayuthapani, Subramanian ; Hart, P. John. / Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine. In: Journal of Bacteriology. 2003 ; Vol. 185, No. 14. pp. 4119-4126.
@article{e6932959c03d469c8d941fcc1f25af62,
title = "Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine",
abstract = "Peptide methionine sulfoxide reductase (MsrA) repairs oxidative damage to methionine residues arising from reactive oxygen species and reactive nitrogen intermediates. MsrA activity is found in a wide variety of organisms, and it is implicated as one of the primary defenses against oxidative stress. Disruption of the gene encoding MsrA in several pathogenic bacteria responsible for infections in humans results in the loss of their ability to colonize host cells. Here, we present the X-ray crystal structure of MsrA from the pathogenic bacterium Mycobacterium tuberculosis refined to 1.5 {\AA} resolution. In contrast to the three catalytic cysteine residues found in previously characterized MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. The structure reveals a methionine residue of one MsrA molecule bound at the active site of a neighboring molecule in the crystal lattice and thus serves as an excellent model for protein-bound methionine sulfoxide recognition and repair.",
author = "Taylor, {Alexander B.} and Benglis, {David M.} and Subramanian Dhandayuthapani and Hart, {P. John}",
year = "2003",
month = "7",
doi = "10.1128/JB.185.14.4119-4126.2003",
language = "English (US)",
volume = "185",
pages = "4119--4126",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "14",

}

TY - JOUR

T1 - Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine

AU - Taylor, Alexander B.

AU - Benglis, David M.

AU - Dhandayuthapani, Subramanian

AU - Hart, P. John

PY - 2003/7

Y1 - 2003/7

N2 - Peptide methionine sulfoxide reductase (MsrA) repairs oxidative damage to methionine residues arising from reactive oxygen species and reactive nitrogen intermediates. MsrA activity is found in a wide variety of organisms, and it is implicated as one of the primary defenses against oxidative stress. Disruption of the gene encoding MsrA in several pathogenic bacteria responsible for infections in humans results in the loss of their ability to colonize host cells. Here, we present the X-ray crystal structure of MsrA from the pathogenic bacterium Mycobacterium tuberculosis refined to 1.5 Å resolution. In contrast to the three catalytic cysteine residues found in previously characterized MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. The structure reveals a methionine residue of one MsrA molecule bound at the active site of a neighboring molecule in the crystal lattice and thus serves as an excellent model for protein-bound methionine sulfoxide recognition and repair.

AB - Peptide methionine sulfoxide reductase (MsrA) repairs oxidative damage to methionine residues arising from reactive oxygen species and reactive nitrogen intermediates. MsrA activity is found in a wide variety of organisms, and it is implicated as one of the primary defenses against oxidative stress. Disruption of the gene encoding MsrA in several pathogenic bacteria responsible for infections in humans results in the loss of their ability to colonize host cells. Here, we present the X-ray crystal structure of MsrA from the pathogenic bacterium Mycobacterium tuberculosis refined to 1.5 Å resolution. In contrast to the three catalytic cysteine residues found in previously characterized MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. The structure reveals a methionine residue of one MsrA molecule bound at the active site of a neighboring molecule in the crystal lattice and thus serves as an excellent model for protein-bound methionine sulfoxide recognition and repair.

UR - http://www.scopus.com/inward/record.url?scp=0038154089&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038154089&partnerID=8YFLogxK

U2 - 10.1128/JB.185.14.4119-4126.2003

DO - 10.1128/JB.185.14.4119-4126.2003

M3 - Article

VL - 185

SP - 4119

EP - 4126

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 14

ER -