1ix5: Difference between revisions

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{{STRUCTURE_1ix5|  PDB=1ix5  |  SCENE=  }}  
{{STRUCTURE_1ix5|  PDB=1ix5  |  SCENE=  }}  


'''Solution structure of the Methanococcus thermolithotrophicus FKBP'''
===Solution structure of the Methanococcus thermolithotrophicus FKBP===




==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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==About this Structure==
==About this Structure==
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].  
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 14:09, 1 July 2008

File:1ix5.png

Template:STRUCTURE 1ix5

Solution structure of the Methanococcus thermolithotrophicus FKBPSolution structure of the Methanococcus thermolithotrophicus FKBP

Template:ABSTRACT PUBMED 12729748

About this StructureAbout this Structure

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

ReferenceReference

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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