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Crystallization and preliminary X-ray crystallographic studies of enoyl-acyl carrier protein reductase (FabI) from Psuedomonas aeruginosa

Authors
Lee, Jeong HyePark, Ae KyungChi, Young MinMoon, Jin HoLee, Ki Seog
Issue Date
2월-2011
Publisher
INT UNION CRYSTALLOGRAPHY
Keywords
Enoyl-acyl carrier protein reductases; FabI; Fatty-acid synthesis; Pseudomonas aeruginosa; Triclosan
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.67, pp.214 - 216
Indexed
SCOPUS
Journal Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume
67
Start Page
214
End Page
216
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/113118
DOI
10.1107/S1744309110048827
ISSN
2053-230X
Abstract
During fatty-acid biosynthesis, enoyl-acyl carrier protein (enoyl-ACP) reductase catalyzes the reduction of trans-2-enoyl-ACP to fully saturated acyl-ACP via the ubiquitous fatty-acid synthase system. NADH-dependent enoyl-ACP reductase (FabI) from Pseudomonas aeruginosa has been purified and crystallized as an apoenzyme and in a complex form with NADH and triclosan. Triclosan is an inhibitor of FabI and forms a stable ternary complex in the presence of NADH. The crystals of native and complexed FabI diffracted to resolutions of 2.6 and 1.8 angstrom, respectively. The crystals both belonged to space group P2(1), with unit-cell parameters a = 117.32, b = 155.844, c = 129.448 angstrom, beta = 111.061 degrees for the native enzyme and a = 64.784, b = 107.573, c = 73.517 angstrom, beta = 116.162 degrees for the complex. Preliminary molecular replacement further confirmed the presence of four tetramers of native FabI and one tetramer of the complex in the asymmetric unit, corresponding to Matthews coefficients (V-M) of 2.46 and 2.05 angstrom(3) Da(-1) and solvent contents of 50.1 and 40.1%, respectively.
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생명과학대학 (생명공학부)
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