The structure of ferricytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H

• Published in: Metallomics Vol. 6; no. 6; pp. 1126 - 1130
• Main Authors: Harvilla, Paul B, Wolcott, Holly N, Magyar, John S
• Format: Journal Article
• Language: English
• Published: England 01-06-2014
• Subjects: Alteromonadaceae - chemistry; Bacterial Proteins - chemistry; Crystallography, X-Ray; Cytochrome c Group - chemistry; Models, Molecular; Protein Conformation
• ISSN: 1756-5901; 1756-591X
• DOI: 10.1039/c4mt00045e

Approximately 40% of all proteins are metalloproteins, and approximately 80% of Earth's ecosystems are at temperatures ≤5 °C, including 90% of the global ocean. Thus, an essential aspect of marine metallobiochemistry is an understanding of the structure, dynamics, and mechanisms of cold adaptation of metalloproteins from marine microorganisms. Here, the molecular structure of the electron-transfer protein cytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H has been determined by X-ray crystallography (PDB: ). The structure is highly superimposable with that of the homologous cytochrome from the mesophile Marinobacter hydrocarbonoclasticus. Based on structural analysis and comparison of psychrophilic, psychrotolerant, and mesophilic sequences, a methionine-based ligand-substitution mechanism for psychrophilic protein stabilization is proposed.