The structure of ferricytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H. 2014

Paul B Harvilla, and Holly N Wolcott, and John S Magyar
Department of Chemistry, Barnard College, Columbia University, 3009 Broadway, New York NY 10027, USA. jmagyar@barnard.edu.

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.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D003574 Cytochrome c Group A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539) Cytochromes Type c,Group, Cytochrome c,Type c, Cytochromes
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D018360 Crystallography, X-Ray The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) X-Ray Crystallography,Crystallography, X Ray,Crystallography, Xray,X Ray Crystallography,Xray Crystallography,Crystallographies, X Ray,X Ray Crystallographies
D034241 Alteromonadaceae A family of marine, gram-negative PROTEOBACTERIA including the genera ALTEROMONAS; Colwellia; Idiomarina; MARINOBACTER; MORITELLA; PSEUDOALTEROMONAS; and SHEWANELLA. Colwellia,Idiomarina

Related Publications

Paul B Harvilla, and Holly N Wolcott, and John S Magyar
February 2018, Environmental microbiology reports,
Paul B Harvilla, and Holly N Wolcott, and John S Magyar
January 2015, Journal of the American Chemical Society,
Paul B Harvilla, and Holly N Wolcott, and John S Magyar
October 2017, Biochemical and biophysical research communications,
Paul B Harvilla, and Holly N Wolcott, and John S Magyar
August 2016, Bioscience, biotechnology, and biochemistry,
Paul B Harvilla, and Holly N Wolcott, and John S Magyar
November 2012, Extremophiles : life under extreme conditions,
Paul B Harvilla, and Holly N Wolcott, and John S Magyar
December 2016, Journal of microbiology and biotechnology,
Paul B Harvilla, and Holly N Wolcott, and John S Magyar
June 2006, Extremophiles : life under extreme conditions,
Paul B Harvilla, and Holly N Wolcott, and John S Magyar
July 2015, Extremophiles : life under extreme conditions,
Paul B Harvilla, and Holly N Wolcott, and John S Magyar
August 2013, Acta crystallographica. Section F, Structural biology and crystallization communications,
Copied contents to your clipboard!