Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus
- Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus
- 김수진; 하병학; 김국한; 홍승곤; 신계정; 서세원; 김은경
- Fatty acid biosynthesis; Enoyl-ACP reductase; Dimer; Tetramer; Crystal structure
- Issue Date
- Biochemical and biophysical research communications
- VOL 400, NO 4, 517-522
- Enoyl-[acyl carrier protein] reductase (ENR) is an essential enzyme in type II fatty-acid synthesis that catalyzes
the last step in each elongation cycle. Thus far FabI, FabL and FabK have been reported to carry out
the reaction, with FabI being the most characterized. Some bacteria have more than one ENR, and Bacillus
cereus has two (FabI and FabL) reported. Here, we have determined the crystal structures of the later in
the apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor. The two
structures are almost identical, except for the three stretches that are disordered in the apo form. The apo
form exists as a homo-dimer in both crystal and solution, while the ternary complex forms a homo-tetramer.
The three stretches disordered in the apo structure are important in the cofactor and the inhibitor
binding as well as in tetramer formation.
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