Structure of laccase from Streptomyces coelicolor after soaking with potassium hexacyanoferrate and at an improved resolution of 2.3 Å
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
21206017
PubMed Central
PMC3079965
DOI
10.1107/s1744309110046099
PII: S1744309110046099
Knihovny.cz E-zdroje
- MeSH
- bakteriální proteiny chemie MeSH
- barva MeSH
- ferrikyanidy chemie MeSH
- konformace proteinů * MeSH
- krystalografie rentgenová MeSH
- lakasa chemie MeSH
- měď chemie MeSH
- molekulární modely MeSH
- molekulární sekvence - údaje MeSH
- stabilita enzymů MeSH
- Streptomyces coelicolor enzymologie MeSH
- vazebná místa MeSH
- železo chemie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bakteriální proteiny MeSH
- ferrikyanidy MeSH
- lakasa MeSH
- měď MeSH
- potassium ferricyanide MeSH Prohlížeč
- železo 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