3OID

Crystal Structure of Enoyl-ACP Reductases III (FabL) from B. subtilis (complex with NADP and TCL)

Summary for 3OID

• Entry DOI: 10.2210/pdb3oid/pdb
• Related: 3OIC 3OIF 3OIG
• Descriptor: Enoyl-[acyl-carrier-protein] reductase [NADPH], TRICLOSAN, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: fatty acid synthesis, enoyl-acp reductases, fabl, rossmann-like fold, nadph binding, oxidoreductase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 4
• Total formula weight: 117265.63

Authors

Kim, K.-H.,Ha, B.H.,Kim, S.J.,Hong, S.K.,Hwang, K.Y.,Kim, E.E. (deposition date: 2010-08-19, release date: 2011-01-05, Last modification date: 2023-11-01)

Primary citation

Kim, K.-H.,Ha, B.H.,Kim, S.J.,Hong, S.K.,Hwang, K.Y.,Kim, E.E.
Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis
J.Mol.Biol., 406:403-415, 2011

PubMed Abstract: Enoyl-[acyl carrier protein] (ACP) reductase (ENR) is a key enzyme in type II fatty acid synthesis that catalyzes the last step in each elongation cycle. Therefore, it has been considered as a target for antibiotics. However, recent studies indicate that some pathogens have more than one ENR; in particular, Bacillus subtilis has two ENRs, FabI and FabL. The crystal structures of the ternary complexes of BsFaBI and BsFabL are found as a homotetramer showing the same overall structure despite a sequence identity of only 24%. The positions of the catalytic dyad of Tyr-(Xaa)(6)-Lys in FabL are almost identical to that of FabI, but a detailed structural analysis shows that FabL shares more structural similarities with FabG and other members of the SDR (short-chain alcohol dehydrogenase/reductase) family. The apo FabL structure shows significantly different conformations at the cofactor and the substrate-binding regions, and this resulted in a totally different tetrameric arrangement reflecting the flexibility of these regions in the absence of the cofactor and substrate/inhibitor.

PubMed: 21185310
DOI: 10.1016/j.jmb.2010.12.003

Experimental method

X-RAY DIFFRACTION (1.8 Å)