Structural analysis of 1-Cys type selenoprotein methionine sulfoxide reductase A

Title
Structural analysis of 1-Cys type selenoprotein methionine sulfoxide reductase A
Author(s)
김화영이은혜[이은혜]곽근희김문정황광연[황광연]
Keywords
PROTEIN-BOUND METHIONINE; CATALYTIC MECHANISM; ESCHERICHIA-COLI; NEISSERIA-MENINGITIDIS; ANTIOXIDANT DEFENSE; SULFENIC ACID; AMINO-ACIDS; MSRA; SELENOCYSTEINE; OXIDATION
Issue Date
201403
Publisher
ELSEVIER SCIENCE INC
Citation
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, v.545, pp.1 - 8
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 1.6-1.8 angstrom, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure of Clostridium MsrA, consisting of ten alpha-helices and six beta-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. (C) 2014 Elsevier Inc. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/32811http://dx.doi.org/10.1016/j.abb.2013.12.024
ISSN
0003-9861
Appears in Collections:
의과대학 > 생화학.분자생물학교실 > Articles
의과대학 > 영상의학과학교실 > Articles
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