4NFG

K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex

Summary for 4NFG

• Entry DOI: 10.2210/pdb4nfg/pdb
• Descriptor: Cytochrome c peroxidase, mitochondrial, Cytochrome c, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• Functional Keywords: oxidoreductase/electron transport, oxidoreductase-electron transport complex
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Mitochondrion matrix: P00431; Mitochondrion intermembrane space: P00004
• Total number of polymer chains: 2
• Total formula weight: 46541.85

Authors

Meulenbroek, E.M.,Bashir, Q.,Ubbink, M.,Pannu, N.S. (deposition date: 2013-10-31, release date: 2014-09-24, Last modification date: 2024-11-27)

Primary citation

Bashir, Q.,Meulenbroek, E.M.,Pannu, N.S.,Ubbink, M.
Engineering specificity in a dynamic protein complex with a single conserved mutation.
Febs J., 281:4892-4905, 2014

PubMed Abstract: It has been demonstrated that the complex of yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP) exists as a delicate equilibrium of a specific, active state and the non-specific, dynamic encounter state. An ortholog of yeast Cc, horse Cc, binds CcP but forms a much more dynamic complex, as demonstrated by NMR spectroscopy. A single conservative mutation of lysine 13 to arginine reduces the dynamics and enhances the specificity. The crystal structure of the stereospecific complex resembles the yeast Cc-CcP complex. In contrast, the K13A mutation increases the dynamic nature of the complex with CcP, showing that specificity in a redox protein complex can depend on the interactions of a single side chain in the binding interface.

PubMed: 25180929
DOI: 10.1111/febs.13028

Experimental method

X-RAY DIFFRACTION (2.11 Å)