Essential Role of the C-Terminal Helical Domain in Active Site Formation of Selenoprotein MsrA from Clostridium oremlandii

Title
Essential Role of the C-Terminal Helical Domain in Active Site Formation of Selenoprotein MsrA from Clostridium oremlandii
Author(s)
김화영이은혜[이은혜]이기택[이기택]황광연[황광연]
Keywords
METHIONINE SULFOXIDE REDUCTASE; ESCHERICHIA-COLI; CATALYTIC MECHANISM; KINETIC CHARACTERIZATION; NEISSERIA-MENINGITIDIS; EXPRESSION; SYSTEM; ENZYME
Issue Date
201502
Publisher
PUBLIC LIBRARY SCIENCE
Citation
PLOS ONE, v.10, no.2
Abstract
We previously determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii (CoMsrA). The overall structure of CoMsrA is unusual, consisting of two domains, the N-terminal catalytic domain and the C-terminal distinct helical domain which is absent from other known MsrA structures. Deletion of the helical domain almost completely abolishes the catalytic activity of CoMsrA. In this study, we determined the crystal structure of the helical domain-deleted (Delta H-domain) form of CoMsrA at a resolution of 1.76 angstrom. The monomer structure is composed of the central rolled mixed beta-sheet surrounded by a-helices. However, there are significant conformational changes in the N- and C-termini and loop regions of the Delta H-domain protein relative to the catalytic domain structure of full-length CoMsrA. The active site structure in the Delta H-domain protein completely collapses, thereby causing loss of catalytic activity of the protein. Interestingly, dimer structures are observed in the crystal formed by N-terminus swapping between two molecules. The Delta H-domain protein primarily exists as a dimer in solution, whereas the full-length CoMsrA exists as a monomer. Collectively, this study provides insight into the structural basis of the essential role of the helical domain of CoMsrA in its catalysis.
URI
http://hdl.handle.net/YU.REPOSITORY/33431http://dx.doi.org/10.1371/journal.pone.0117836
ISSN
1932-6203
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의과대학 > 생화학.분자생물학교실 > Articles
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