Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 328, Issue 5, Pages 1149-1160Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/S0022-2836(03)00379-6
Keywords
FKBP; peptidyl-prolyl cis-trans isomerase; chaperone; archaea; NMR structure determination
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Here we report the solution structure of an archaeal FK506-binding protein (FKBP) from a thermophilic archaeum, Methanococcus thermolithotrophicus (MtFKBP17), which has peptidyl prolyl cis-trans isomerase (PPIase) and chaperone-like activities, to reveal the structural basis for the dual function. In addition to a typical PPIase domain, a newly identified domain is formed in the flap loop by a 48-residue insert that is required for the chaperone-like activity. The new domain, called IF domain (the Insert in the Flap), is a novel-folding motif and exposes a hydrophobic surface, which we consider to play an important role in the chaperone-like activity. (C) 2003 Published by Elsevier Science Ltd.
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