2GEW
Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)
Summary for 2GEW
| Entry DOI | 10.2210/pdb2gew/pdb |
| Descriptor | Cholesterol oxidase, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | flavoenzyme, steroid metabolism, oxidoreductase, atomic resolution, hydrogen bond |
| Biological source | Streptomyces sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 55883.29 |
| Authors | Lyubimov, A.Y.,Vrielink, A. (deposition date: 2006-03-20, release date: 2006-05-02, Last modification date: 2023-08-30) |
| Primary citation | Lyubimov, A.Y.,Lario, P.I.,Moustafa, I.,Vrielink, A. Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment. Nat.Chem.Biol., 2:259-264, 2006 Cited by PubMed Abstract: Hydrogen atoms are a vital component of enzyme structure and function. In recent years, atomic resolution crystallography (>or=1.2 A) has been successfully used to investigate the role of the hydrogen atom in enzymatic catalysis. Here, atomic resolution crystallography was used to study the effect of pH on cholesterol oxidase from Streptomyces sp., a flavoenzyme oxidoreductase. Crystallographic observations of the anionic oxidized flavin cofactor at basic pH are consistent with the UV-visible absorption profile of the enzyme and readily explain the reversible pH-dependent loss of oxidation activity. Furthermore, a hydrogen atom, positioned at an unusually short distance from the main chain carbonyl oxygen of Met122 at high pH, was observed, suggesting a previously unknown mechanism of cofactor stabilization. This study shows how a redox active site responds to changes in the enzyme's environment and how these changes are able to influence the mechanism of enzymatic catalysis. PubMed: 16604066DOI: 10.1038/nchembio784 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.97 Å) |
Structure validation
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