1ix5
From Proteopedia
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'''Solution structure of the Methanococcus thermolithotrophicus FKBP''' | '''Solution structure of the Methanococcus thermolithotrophicus FKBP''' | ||
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[[Category: Suzuki, R.]] | [[Category: Suzuki, R.]] | ||
[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
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Revision as of 17:31, 2 May 2008
Solution structure of the Methanococcus thermolithotrophicus FKBP
Overview
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.
About this Structure
1IX5 is a Single protein structure of sequence from Methanothermococcus thermolithotrophicus. Full crystallographic information is available from OCA.
Reference
Three-dimensional solution structure of an archaeal FKBP with a dual function of peptidyl prolyl cis-trans isomerase and chaperone-like activities., Suzuki R, Nagata K, Yumoto F, Kawakami M, Nemoto N, Furutani M, Adachi K, Maruyama T, Tanokura M, J Mol Biol. 2003 May 16;328(5):1149-60. PMID:12729748 Page seeded by OCA on Fri May 2 20:31:54 2008
