› 3zgn

X-ray diffraction
1.95Å resolution

Crystal structures of Escherichia coli IspH in complex with TMBPP a potent inhibitor of the methylerythritol phosphate pathway

Released:
DOI: 10.2210/pdb3zgn/pdb
PDB entry 3zgn coloured by chain, front view.
PDB entry 3zgn coloured by chain, side view.
PDB entry 3zgn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Further Insight into Crystal Structures of Escherichia coli IspH/LytB in Complex with Two Potent Inhibitors of the MEP Pathway: A Starting Point for Rational Design of New Antimicrobials.
Borel F, Barbier E, Krasutsky S, Janthawornpong K, Chaignon P, Poulter CD, Ferrer JL, Seemann M
Chembiochem 18 2137-2144 (2017)
PMID: 28862365

Function and Biology Details

Reaction catalysed: 
Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158657 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-3-methylbut-2-enyl diphosphate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 36.64 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli M15
UniProt:
  • Canonical: P62623 (Residues: 1-316; Coverage: 100%)
Gene names: JW0027, b0029, ispH, lytB, yaaE
Sequence domains: LytB protein
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 10G 2 x 10G
Ligand SF4 2 x SF4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 112.39Å b: 80.57Å c: 70.62Å
α: 90° β: 94.46° γ: 90°
R-values:
R R work R free
0.207 0.205 0.258
Expression system: Escherichia coli M15

Quick links

Citations

2 mentions without citation

The Reductive Dehydroxylation Catalyzed by IspH, a Source of Inspiration for the Development of Novel Anti-Infectives.
Jobelius et al. (2022)
1 more