Structural highlights
1n1p is a 1 chain structure with sequence from Chainia sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Related: | 1b4v, 1mxt, 1b8s, 1cc2, 1ijh, 1cbo, 1n4v, 1n4w, 1n4u |
| Gene: | CHOA (Chainia sp.) |
| Activity: | Cholesterol oxidase, with EC number 1.1.3.6 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[CHOD_STRS0] Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The X-ray crystal structure of the flavoenzyme cholesterol oxidase, SCOA (Streptomyces sp.SA-COO) has been determined to 0.95 A resolution. The large size (55kDa) and the high-resolution diffraction of this protein provides a unique opportunity to observe detailed electronic effects within a protein environment and to obtain a larger sampling for which to analyze these electronic and structural differences. It is well-known through spectroscopic methods that peptide carbonyl groups are polarized in alpha-helices. This electronic characteristic is evident in the sub-Angstrom electron density of SCOA. Our analysis indicates an increased tendency for the electron density of the main chain carbonyl groups within alpha-helices to be polarized toward the oxygen atoms. In contrast, the carbonyl groups in beta-sheet structures tend to exhibit a greater charge density between the carbon and oxygen atoms. Interestingly, the electronic differences observed at the carbonyl groups do not appear to be correlated to the bond distance of the peptide bond or the peptide planarity. This study gives important insight into the electronic effects of alpha-helix dipoles in enzymes and provides experimentally based observations that have not been previously characterized in protein structure.
Atomic resolution density maps reveal secondary structure dependent differences in electronic distribution.,Lario PI, Vrielink A J Am Chem Soc. 2003 Oct 22;125(42):12787-94. PMID:14558826[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lario PI, Vrielink A. Atomic resolution density maps reveal secondary structure dependent differences in electronic distribution. J Am Chem Soc. 2003 Oct 22;125(42):12787-94. PMID:14558826 doi:10.1021/ja0289954
