This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ix5
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1ix5.jpg|left|200px]] | [[Image:1ix5.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1ix5", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1ix5| PDB=1ix5 | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Solution structure of the Methanococcus thermolithotrophicus FKBP''' | '''Solution structure of the Methanococcus thermolithotrophicus FKBP''' | ||
| Line 34: | Line 31: | ||
[[Category: Suzuki, R.]] | [[Category: Suzuki, R.]] | ||
[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
| - | [[Category: | + | [[Category: Fkbp fold]] |
| - | [[Category: | + | [[Category: Ppiase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:31:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
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
