Role of the Unique Peptide Tail in Hyperthermostable Aquifex aeolicus Cochaperonin Protein 10

• Published in: Biochemistry (Easton) Vol. 44; no. 44; pp. 14385 - 14395
• Main Authors: Luke, Kathryn, Apiyo, David, Wittung-Stafshede, Pernilla
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 08.11.2005
• Subjects: Bacteria - chemistry; Bacteria - genetics; Chaperonin 10 - chemistry; Chaperonin 10 - genetics; Chaperonin 10 - metabolism; Chaperonin 10 - ultrastructure; Hot Temperature; Models, Molecular; Peptides - chemistry; Peptides - genetics; Peptides - metabolism; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits - chemistry; Protein Subunits - genetics; Protein Subunits - metabolism; Thermodynamics

All known cochaperonin protein 10 (cpn10) molecules are heptamers of seven identical subunits noncovalently linked by β-strand interactions. Cpn10 from the deep-branching, hyperthermophilic bacterium Aquifex aeolicus (Aacpn10) shows high homology with mesophilic and other thermophilic cpn10 sequence...