4LWJ

Crystal structure of methionine sulfoxide reductase U16C from clostridium oremlandii

Summary for 4LWJ

• Entry DOI: 10.2210/pdb4lwj/pdb
• Related: 4LWK 4LWL 4LWM 4LWN
• Descriptor: Peptide methionine sulfoxide reductase MsrA, ACETATE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: alpha/beta fold, peptide-methionine (s)-s-oxide reductase, oxidoreductase
• Biological source: Alkaliphilus oremlandii
• Total number of polymer chains: 1
• Total formula weight: 24971.86

Authors

Hwang, K.Y.,Lee, E.H. (deposition date: 2013-07-27, release date: 2014-06-11, Last modification date: 2024-10-30)

Primary citation

Lee, E.H.,Kwak, G.H.,Kim, M.J.,Kim, H.Y.,Hwang, K.Y.
Structural analysis of 1-Cys type selenoprotein methionine sulfoxide reductase A
Arch.Biochem.Biophys., 545:1-8, 2014

PubMed Abstract: Methionine sulfoxide reductase A (MsrA) reduces free and protein-based methionine-S-sulfoxide to methionine. Structures of 1-Cys MsrAs lacking a resolving Cys, which interacts with catalytic Cys, are unknown. In addition, no structural information on selenocysteine (Sec)-containing MsrA enzymes has been reported. In this work, we determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii at 1.6-1.8Å, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure of Clostridium MsrA, consisting of ten α-helices and six β-strands, folds into a catalytic domain and a novel helical domain absent from other known MsrA structures. The helical domain, containing five helices, tightly interacts with the catalytic domain, and is likely critical for catalytic activity due to its association with organizing the active site. This helical domain is also conserved in several selenoprotein MsrAs. Our structural analysis reveals that the side chain length of Glu55 is critical for the proton donor function of this residue. Our structures also provide insights into the architecture of the 1-Cys MsrA active site and the roles of active site residues in substrate recognition and catalysis.

PubMed: 24412203
DOI: 10.1016/j.abb.2013.12.024

Experimental method

X-RAY DIFFRACTION (1.8 Å)