1ix5

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{{STRUCTURE_1ix5| PDB=1ix5 | SCENE= }}
{{STRUCTURE_1ix5| PDB=1ix5 | SCENE= }}
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'''Solution structure of the Methanococcus thermolithotrophicus FKBP'''
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===Solution structure of the Methanococcus thermolithotrophicus FKBP===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_12729748}}
==About this Structure==
==About this Structure==
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1IX5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA].
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1IX5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA].
==Reference==
==Reference==
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[[Category: Fkbp fold]]
[[Category: Fkbp fold]]
[[Category: Ppiase]]
[[Category: Ppiase]]
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Revision as of 11:09, 1 July 2008

Image:1ix5.png

Template:STRUCTURE 1ix5

Solution structure of the Methanococcus thermolithotrophicus FKBP

Template:ABSTRACT PUBMED 12729748

About this Structure

1IX5 is a Single protein structure of sequence from Methanothermococcus thermolithotrophicus. Full experimental 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

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