› 4i52

X-ray diffraction
2.35Å resolution

scMenB im complex with 1-hydroxy-2-naphthoyl-CoA

Released:
DOI: 10.2210/pdb4i52/pdb
PDB entry 4i52 coloured by chain, front view.
PDB entry 4i52 coloured by chain, side view.
PDB entry 4i52 coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6803 substr. Kazusa
Primary publication:
Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme A synthase from the crotonase fold superfamily.
Sun Y, Song H, Li J, Li Y, Jiang M, Zhou J, Guo Z
PLoS One 8 e63095 (2013)
PMID: 23658663

Function and Biology Details

Reaction catalysed: 
4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159897 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1,4-dihydroxy-2-naphthoyl-CoA synthase Chains: A, B, C, D, E, F, G, H, I
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I
Length: 275 amino acids
Theoretical weight: 30.34 KDa
Source organism: Synechocystis sp. PCC 6803 substr. Kazusa
UniProt:
  • Canonical: P73495 (Residues: 1-275; Coverage: 100%)
Gene name: menB
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments


Cofactor: Ligand 1HA 9 x 1HA
1 bound ligand:
Ligand CL 9 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P3221
Unit cell:
a: 138.843Å b: 138.843Å c: 221.217Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.229 0.256

Quick links

Citations

2 citation in other articles

A Methyl 4-Oxo-4-phenylbut-2-enoate with in Vivo Activity against MRSA that Inhibits MenB in the Bacterial Menaquinone Biosynthesis Pathway.
Matarlo et al. (2016)
1 more

1 mention without citation

Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme A synthase from the crotonase fold superfamily.
Sun et al. (2013)