Structural highlights
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
A proposed electron transfer pathway in cytochrome c peroxidase was previously excised from the structure by design. The engineered channel mutant was shown to bind peptide surrogates without restoration of cyt c oxidation. Here, we report the 1.6 A crystal structure of (N-benzimidazole-propionic acid)-Gly-Ala-Ala bound within the engineered channel. The peptide retains many features of the native electron transfer pathway: placement of benzimidazole at the position of the Trp-191 radical, hydrogen bonding to Asp235, and positioning of the C-terminus near the point where wild type CcP makes closest contact to cyt c. The inability of this surrogate pathway to restore function supports proposals that electron transfer requires the Trp-191 radical.
Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide.,Hays Putnam AM, Lee YT, Goodin DB Biochemistry. 2009 Jan 13;48(1):1-3. PMID:19072042[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hays Putnam AM, Lee YT, Goodin DB. Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide. Biochemistry. 2009 Jan 13;48(1):1-3. PMID:19072042 doi:10.1021/bi8020263
