Kim, Kook-Han Park, Joon Kyu Ha, Byung Hak Moon, Jin Ho Kim, Eunice EunKyeong 2024-01-21T01:31:43Z 2024-01-21T01:31:43Z 2021-09-04 2007-03 2053-230X https://pubs.kist.re.kr/handle/201004/134614 Enoyl-[acyl-carrierprotein] reductase (enoyl-ACP reductase; ENR) is a key enzyme in type II fatty-acid synthase that catalyzes the last step in each elongation cycle. It has been considered as an antibiotic target since it is an essential enzyme in bacteria. However, recent studies indicate that some pathogens have more than one ENR. Bacillus subtilis is reported to have two ENRs, namely BsFabI and BsFabL. While BsFabI is similar to other FabIs, BsFabL shows very little sequence similarity and is NADPH-dependent instead of NADH-dependent as in the case of FabI. In order to understand these differences on a structural basis, BsFabL has been cloned, expressed and and crystallized. The crystal belongs to space group P622, with unit-cell parameters a = b = 139.56, c = 62.75 angstrom, alpha = beta = 90, gamma = 120 degrees and one molecule of FabL in the asymmetric unit. Data were collected using synchrotron radiation (beamline 4A at the Pohang Light Source, Korea). The crystal diffracted to 2.5 angstrom resolution. English INT UNION CRYSTALLOGRAPHY ACYL CARRIER PROTEIN FATTY-ACID BIOSYNTHESIS MYCOBACTERIUM-TUBERCULOSIS ESCHERICHIA-COLI ANTIBACTERIAL AGENTS TRICLOSAN INHIBITION INHA ELONGATION MECHANISM Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis Article 10.1107/S1744309107008469 1 ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.63, pp.246 - 248 ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 63 246 248 scie scopus 000244520800023 2-s2.0-33947305001 Biochemical Research Methods Biochemistry & Molecular Biology Biophysics Crystallography Biochemistry & Molecular Biology Biophysics Crystallography Article ACYL CARRIER PROTEIN FATTY-ACID BIOSYNTHESIS MYCOBACTERIUM-TUBERCULOSIS ESCHERICHIA-COLI ANTIBACTERIAL AGENTS TRICLOSAN INHIBITION INHA ELONGATION MECHANISM Antibacterial drug targets Bacillus subtilis Enoyl-ACP reductase FabL Fatty-acid synthesis