| Structural highlights
3m2a is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Related: | 1dso, 2v23, 1dsg, 1zby, 5ccp, 3e2n, 3e2o, 3m23, 3m25, 3m26, 3m27, 3m28, 3m29, 3m2b, 3m2c, 3m2d, 3m2e, 3m2f, 3m2g, 3m2h, 3m2i |
| Gene: | CCP, CCP1, CPO, YKR066C (Saccharomyces cerevisiae) |
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Function
[CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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 ferryl [Fe(IV)O] intermediate is important in many heme enzymes, and thus, the precise nature of the Fe(IV)-O bond is critical in understanding enzymatic mechanisms. The 1.40 A crystal structure of cytochrome c peroxidase Compound I has been determined as a function of X-ray dose while the visible spectrum was being monitored. The Fe-O bond increases in length from 1.73 A in the low-X-ray dose structure to 1.90 A in the high-dose structure. The low-dose structure correlates well with an Fe(IV) horizontal lineO bond, while we postulate that the high-dose structure is the cryo-trapped Fe(III)-OH species previously thought to be an Fe(IV)-OH species.
Crystallographic and single-crystal spectral analysis of the peroxidase ferryl intermediate.,Meharenna YT, Doukov T, Li H, Soltis SM, Poulos TL Biochemistry. 2010 Apr 13;49(14):2984-6. PMID:20230048[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Meharenna YT, Doukov T, Li H, Soltis SM, Poulos TL. Crystallographic and single-crystal spectral analysis of the peroxidase ferryl intermediate. Biochemistry. 2010 Apr 13;49(14):2984-6. PMID:20230048 doi:10.1021/bi100238r
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