4O1W

Crystal Structure of Colwellia psychrerythraea cytochrome c

Summary for 4O1W

• Entry DOI: 10.2210/pdb4o1w/pdb
• Descriptor: Cytochrome c552, HEME C, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: cytochrome c, electron transport
• Biological source: Colwellia psychrerythraea
• Total number of polymer chains: 6
• Total formula weight: 53366.16

Authors

Harvilla, P.B.,Wolcott, H.N.,Magyar, J.S.,Shapiro, L.S. (deposition date: 2013-12-16, release date: 2014-04-23, Last modification date: 2023-09-20)

Primary citation

Harvilla, P.B.,Wolcott, H.N.,Magyar, J.S.
The structure of ferricytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H.
Metallomics, 6:1126-1130, 2014

PubMed 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: ). 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.

PubMed: 24727932
DOI: 10.1039/c4mt00045e

Experimental method

X-RAY DIFFRACTION (2 Å)