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3OJF

Crystal Structure of the Bacillus cereus Enoyl-Acyl Carrier Protein Reductase with NADP+ and indole naphthyridinone (Complex form)

Summary for 3OJF
Entry DOI10.2210/pdb3ojf/pdb
Related3OJE
DescriptorEnoyl-[acyl-carrier-protein] reductase (FabL) (NADPH), (2E)-N-[(1,2-dimethyl-1H-indol-3-yl)methyl]-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl)prop-2-enamide, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
Functional Keywordsenoyl-acp reductase, tetramer, rossmann fold, nad(p) binding, oxidoreductase
Biological sourceBacillus cereus
Total number of polymer chains4
Total formula weight116077.87
Authors
Kim, S.J.,Ha, B.H.,Kim, K.H.,Hong, S.K.,Suh, S.W.,Kim, E.E. (deposition date: 2010-08-22, release date: 2010-09-08, Last modification date: 2023-11-01)
Primary citationKim, S.J.,Ha, B.H.,Kim, K.H.,Hong, S.K.,Shin, K.J.,Suh, S.W.,Kim, E.E.
Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus
Biochem.Biophys.Res.Commun., 400:517-522, 2010
Cited by
PubMed Abstract: 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.
PubMed: 20800575
DOI: 10.1016/j.bbrc.2010.08.083
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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数据于2025-06-18公开中

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