1NWA

Structure of Mycobacterium tuberculosis Methionine Sulfoxide Reductase A in Complex with Protein-bound Methionine

Summary for 1NWA

• Entry DOI: 10.2210/pdb1nwa/pdb
• Descriptor: Peptide methionine sulfoxide reductase msrA (2 entities in total)
• Functional Keywords: peptide methionine sulfoxide reductase, oxidoreductase, product complex, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 23041.45

Authors

Taylor, A.B.,Benglis Jr., D.M.,Dhandayuthapani, S.,Hart, P.J.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2003-02-05, release date: 2003-07-08, Last modification date: 2023-08-16)

Primary citation

Taylor, A.B.,Benglis Jr., D.M.,Dhandayuthapani, S.,Hart, P.J.
Structure of Mycobacterium tuberculosis Methionine Sulfoxide Reductase A in Complex with Protein-bound Methionine
J.Bacteriol., 185:4119-4126, 2003

PubMed 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 A 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.

PubMed: 12837786
DOI: 10.1128/JB.185.14.4119-4126.2003

Experimental method

X-RAY DIFFRACTION (1.5 Å)