Structure and Dynamics of the First Archaeal Parvulin Reveal a New Functionally Important Loop in Parvulin-type Prolyl Isomerases

• Published in: The Journal of biological chemistry Vol. 286; no. 8; pp. 6554 - 6565
• Main Authors: Jaremko, Łukasz, Jaremko, Mariusz, Elfaki, Imadeldin, Mueller, Jonathan W., Ejchart, Andrzej, Bayer, Peter, Zhukov, Igor
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 25.02.2011; American Society for Biochemistry and Molecular Biology
• Subjects: Archaeal Proteins - chemistry; Archaebacteria; Cenarchaeum symbiosum; Cold-adapted Protein; Crenarchaeota - enzymology; Humans; NIMA-Interacting Peptidylprolyl Isomerase; NMR; Nuclear Magnetic Resonance, Biomolecular; Peptidylprolyl Isomerase - chemistry; Prolyl Isomerase; Protein Folding; Protein Structure; Protein Structure and Folding; Protein Structure, Secondary; Structural Homology, Protein; Thaumarchaeota; NMR; Archaebacteria; Cold-adapted Protein; Protein Structure; Thaumarchaeota; Protein Folding; Prolyl Isomerase

Parvulins are a group of peptidyl-prolyl isomerases (PPIases) responsible for important biological processes in all kingdoms of life. The PinA protein from the psychrophilic archaeon Cenarchaeum symbiosum is a parvulin-like PPIase. Due to its striking similarity to the human parvulins Pin1 and Par14...