PDBsum entry 6ihc

Biosynthetic protein

PDB id: 6ihc

Contents

Protein chains

(+ 0 more) 151 a.a.

65 a.a.

Ligands

CIT ×3

PN7

Waters ×303

PDB id:

6ihc

Name:

Biosynthetic protein

Title:

Crystal structure of (3r)-hydroxyacyl-acyl carrier protein dehydratase(fabz) y100a mutant in complex with holo-acp from helicobacter pylori

Structure:

3-hydroxyacyl-[acyl-carrier-protein] dehydratase fabz. Chain: a, b, c, d, e, f. Synonym: (3r)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase, (3r)-hydroxymyristoyl-acp dehydrase,beta-hydroxyacyl-acp dehydratase. Engineered: yes. Holo-form acyl carrier protein (holo-acp). Chain: g. Engineered: yes

Source:

Helicobacter pylori. Campylobacter pylori. Organism_taxid: 210. Gene: fabz, aod77_0202395. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Resolution:

2.40Å R-factor: 0.177 R-free: 0.214

Authors:

S.Q.Shen,L.Zhang,L.Zhang

Key ref:

S.Shen et al. (2019). A back-door Phenylalanine coordinates the stepwise hexameric loading of acyl carrier protein by the fatty acid biosynthesis enzyme β-hydroxyacyl-acyl carrier protein dehydratase (FabZ). Int J Biol Macromol, 128, 5. PubMed id: 30677439 DOI: 10.1016/j.ijbiomac.2019.01.094

Date:

29-Sep-18 Release date: 10-Apr-19

Protein chains

Q5G940  (Q5G940_HELPX) -  3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ from Helicobacter pylori

Seq: 159 a.a.

Struc: 151 a.a.*

Protein chain

B6JLE2  (ACP_HELP2) -  Acyl carrier protein from Helicobacter pylori (strain P12)

Seq: 78 a.a.

Struc: 65 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F: E.C.4.2.1.59 - 3-hydroxyacyl-[acyl-carrier-protein] dehydratase.
• Reaction: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O

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

Key reference

DOI no: 10.1016/j.ijbiomac.2019.01.094

Int J Biol Macromol 128:5 (2019)

PubMed id: 30677439

A back-door Phenylalanine coordinates the stepwise hexameric loading of acyl carrier protein by the fatty acid biosynthesis enzyme β-hydroxyacyl-acyl carrier protein dehydratase (FabZ).

S.Shen, X.Hang, J.Zhuang, L.Zhang, H.Bi, L.Zhang.

ABSTRACT

The fatty acid biosynthesis pathway (FAS) was a fundamental procedure to generate a diversity of lipid components for cellular metabolism in bacteria, while the mechanism of substrate recognition remains unclear. The β-hydroxyacyl-acyl carrier protein dehydratase hexamer (FabZ) is an essential module in the elongation cycle of type-II FAS, catalyzing the dehydration of β-hydroxyacyl-lipid substrate carried by the holo form acyl carrier protein (holo-ACP). We previously elucidated an alternating seesaw-like ACP loading manner within a FabZ dimer subunits, mediated by a front-door residue Tyrosine (Tyr100). Here, we demonstrated that a back-door residue Phenylalanine (Phe83) of FabZ regulates the stepwise hexameric loading of ACP. Our finding represents clues as to the dynamic ACP recognition and catalysis mechanism of dehydratase in fatty acid biosynthesis, and provides critical information for developing antimicrobials targeting the dehydratase module in fatty acid biosynthesis pathway.