› 5u7b

X-ray diffraction
2Å resolution

Crystal structure of a the tin-bound form of MerB formed from Diethyltin.

Released:
DOI: 10.2210/pdb5u7b/pdb
PDB entry 5u7b coloured by chain, front view.
PDB entry 5u7b coloured by chain, side view.
PDB entry 5u7b coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and Biochemical Characterization of Organotin and Organolead Compounds Binding to the Organomercurial Lyase MerB Provide New Insights into Its Mechanism of Carbon-Metal Bond Cleavage.
Wahba HM, Stevenson MJ, Mansour A, Sygusch J, Wilcox DE, Omichinski JG
J Am Chem Soc 139 910-921 (2017)
PMID: 27989130

Function and Biology Details

Reaction catalysed: 
An alkylmercury + H(+) = an alkane + Hg(2+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160120 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkylmercury lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 212 amino acids
Theoretical weight: 23.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P77072 (Residues: 1-212; Coverage: 100%)
Gene name: merB
Sequence domains:
Structure domains: Beta-Lactamase

Ligands and Environments

3 bound ligands:
Ligand BR 1 x BR
Ligand ACT 2 x ACT
Ligand ZN6 2 x ZN6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 37.86Å b: 88.802Å c: 55.01Å
α: 90° β: 97.19° γ: 90°
R-values:
R R work R free
0.171 0.165 0.224
Expression system: Escherichia coli BL21(DE3)

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Citations

2 citation in other articles

Genetic and Physiological Adaptations of Marine Bacterium Pseudomonas stutzeri 273 to Mercury Stress.
Zheng et al. (2018)
1 more

1 mention without citation

Structural and Biochemical Characterization of Organotin and Organolead Compounds Binding to the Organomercurial Lyase MerB Provide New Insights into Its Mechanism of Carbon-Metal Bond Cleavage.
Wahba et al. (2017)