Structure of laccase from Streptomyces coelicolor after soaking with potassium hexacyanoferrate and at an improved resolution of 2.3 Å
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
21206017
PubMed Central
PMC3079965
DOI
10.1107/s1744309110046099
PII: S1744309110046099
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins chemistry MeSH
- Color MeSH
- Ferricyanides chemistry MeSH
- Protein Conformation * MeSH
- Crystallography, X-Ray MeSH
- Laccase chemistry MeSH
- Copper chemistry MeSH
- Models, Molecular MeSH
- Molecular Sequence Data MeSH
- Enzyme Stability MeSH
- Streptomyces coelicolor enzymology MeSH
- Binding Sites MeSH
- Iron chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Ferricyanides MeSH
- Laccase MeSH
- Copper MeSH
- potassium ferricyanide MeSH Browser
- Iron MeSH
The paper reports the structure of the small laccase from Streptomyces coelicolor determined from a crystal soaked with potassium hexacyanoferrate [K4Fe(CN)6]. The decolorization of the natively blue crystal observed upon soaking indicates the reduction of the enzyme in the crystal. The ligand binds between laccase molecules and stabilizes the crystal. The increased diffraction limit of the diffraction data collected from this crystal enabled the refinement of the small laccase structure at 2.3 Å resolution, which is the highest resolution obtained to date.
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PDB
3KW8