3EXB

Crystal structure of Cytochrome C Peroxidase with a Proposed Electron Pathway Excised in a Complex with a Peptide Wire

Summary for 3EXB

• Entry DOI: 10.2210/pdb3exb/pdb
• Related: 1KXM 1KXN
• Related PRD ID: PRD_000453
• Descriptor: Cytochrome c peroxidase, N-[3-(1H-BENZIMIDAZOL-1-YL)PROPANOYL]GLYCYL-L-ALANYL-L-ALANINAMIDE, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, peroxidase, heme, hydrogen peroxide, iron, metal-binding, mitochondrion, transit peptide, oxidoreductase-peptide complex, oxidoreductase/peptide
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 34593.28

Authors

Putnam, A.-M.A.,Lee, Y.-T.,Goodin, D.B. (deposition date: 2008-10-16, release date: 2009-01-13, Last modification date: 2024-10-16)

Primary citation

Hays Putnam, A.M.,Lee, Y.T.,Goodin, D.B.
Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide
Biochemistry, 48:1-3, 2009

PubMed Abstract: 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.

PubMed: 19072042
DOI: 10.1021/bi8020263

Experimental method

X-RAY DIFFRACTION (1.6 Å)