Crystallization and preliminary X-ray crystallographic analysis of the methionine sulfoxide reductase A domain of MsrAB from Haemophilus influenzae

Title
Crystallization and preliminary X-ray crystallographic analysis of the methionine sulfoxide reductase A domain of MsrAB from Haemophilus influenzae
Author(s)
김화영한아름[한아름]김현숙[김현숙]조계윤[조계윤]기호삼[기호삼]황광연[황광연]
Keywords
CATALYTIC MECHANISM; KINETIC CHARACTERIZATION; NEISSERIA-MENINGITIDIS; ESCHERICHIA-COLI; OXIDATION; PROTEIN; REPAIR; ZINC
Issue Date
201205
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.68, pp.557 - 559
Abstract
Methionine sulfoxide reductase (Msr) is a repair enzyme that reduces oxidized methionine to methionine. The Msr enzyme is divided into MsrA and MsrB, which reduce the S and R configurations of the substrate, respectively. In some pathogenic bacteria MsrA and MsrB exist in a fusion-protein form, MsrAB. In this study, the recombinant MsrA part of MsrAB from Haemophilus influenzae (HIMsrA) was overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method. A diffraction data set was collected to 1.6 angstrom resolution. The crystal of HIMsrA was found to belong to space group P4(1)2(1)2, with unit-cell parameters a = b = 57.29, c = 186.28 angstrom, a calculated Matthews coefficient of 1.82 angstrom(3) Da(-1) and two molecules per asymmetric unit. A preliminary solution was determined by molecular replacement. Refinement of the structure is currently in progress.
URI
http://hdl.handle.net/YU.REPOSITORY/28287http://dx.doi.org/10.1107/S1744309112011256
ISSN
1744-3091
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의과대학 > 생화학.분자생물학교실 > Articles
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