PDBsum entry 5ycs

Oxidoreductase

PDB id: 5ycs

Contents

Protein chains

256 a.a.

Ligands

NAD ×4

TCL ×4

SO4 ×2

Waters ×689

PDB id:

5ycs

Name:

Oxidoreductase

Title:

X-ray structure of enoyl-acyl carrier protein reductase from bacillus anthracis with triclosan

Structure:

Enoyl-[acyl-carrier-protein] reductase [nadh] fabi. Chain: a, b, c, d. Synonym: enr,nadh-dependent enoyl-acp reductase. Engineered: yes. Mutation: yes. Other_details: NAD+, triclosan

Source:

Bacillus cereus (strain atcc 14579 / dsm 31 / jcm 2152 / nbrc 15305 / ncimb 9373 / nrrl b-3711). Organism_taxid: 226900. Strain: atcc 14579 / dsm 31 / jcm 2152 / nbrc 15305 / ncimb 9373 / nrrl b-3711. Gene: fabi, bc_1216. Expressed in: escherichia coli-pichia pastoris shuttle vector ppparg4. Expression_system_taxid: 1182032

Resolution:

1.95Å R-factor: 0.161 R-free: 0.190

Authors:

H.T.Kim

Key ref:

H.T.Kim et al. (2017). Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis. Biochem Biophys Res Commun, 493, 28-33. PubMed id: 28935372 DOI: 10.1016/j.bbrc.2017.09.084

Date:

08-Sep-17 Release date: 21-Feb-18

Protein chains

Q81GI3  (FABI_BACCR) -  Enoyl-[acyl-carrier-protein] reductase [NADH] FabI from Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)

Seq: 256 a.a.

Struc: 256 a.a.

Enzyme reactions

• Enzyme class: E.C.1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH).
• Reaction: a 2,3-saturated acyl-[ACP] + NAD⁺ = a (2E)-enoyl-[ACP] + NADH + H⁺

2,3-saturated acyl-[ACP] + NAD(+) (Bound ligand (Het Group name = NAD) corresponds exactly) = (2E)-enoyl-[ACP] + NADH + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/j.bbrc.2017.09.084

Biochem Biophys Res Commun 493:28-33 (2017)

PubMed id: 28935372

Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis.

H.T.Kim, S.Kim, B.K.Na, J.Chung, E.Hwang, K.Y.Hwang.

ABSTRACT

Enoyl-ACP reductase (ENR, also known as FabI) has received considerable interest as an anti-bacterial target due to its essentiality in fatty acid synthesis. All the FabI structures reported to date, regardless of the organism, are composed of homo-tetramers, except for two structures: Bacillus cereus and Staphylococcus aureus FabI (bcFabI and saFabI, respectively), which have been reported as dimers. However, the reason for the existence of the dimeric form in these organisms and the biological meaning of dimeric and tetrameric forms of FabI are ambiguous. Herein, we report the high-resolution crystal structure of a dimeric form of Bacillus anthracis FabI (baFabI) and the crystal structures of tetrameric forms of baFabI in the apo state and in complex with NAD⁺and with NAD⁺-triclosan, at 1.7 Å, 1.85 Å, 1.96 Å, and 1.95 Å, respectively. Interestingly, we found that baFabI with a His₆-tag at its C-terminus exists as a dimer, whereas untagged-baFabI exists as a tetramer. The His₆-tag may block the dimer-tetramer transition, since baFabI has relatively short-length amino acids (²⁵⁵LG²⁵⁶) after the 3₁₀-helix η7 compared to those of FabI of other organisms. The dimeric form of baFabI is catalytically inactive, because the α-helix α5 occupies the NADH-binding site. During the process of dimer-tetramer transition, this α5 helix rotates about 55° toward the tetramer interface and the active site is established. Therefore, tetramerization of baFabI is required for cofactor binding and catalytic activity.