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Issue 6, 2014
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The structure of ferricytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H

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Abstract

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: 4O1W). 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.

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

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Publication details

The article was received on 17 Feb 2014, accepted on 08 Apr 2014 and first published on 09 Apr 2014


Article type: Paper
DOI: 10.1039/C4MT00045E
Author version available: Download Author version (PDF)
Citation: Metallomics, 2014,6, 1126-1130
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    The structure of ferricytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H

    P. B. Harvilla, H. N. Wolcott and J. S. Magyar, Metallomics, 2014, 6, 1126
    DOI: 10.1039/C4MT00045E

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