3PRB

Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26

3PRB の概要

• エントリーDOI: 10.2210/pdb3prb/pdb
• 関連するPDBエントリー: 3PR9 3PRA 3PRD
• 分子名称: FKBP-type peptidyl-prolyl cis-trans isomerase (2 entities in total)
• 機能のキーワード: fkbp, chaperone, isomerase
• 由来する生物種: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51974.69

構造登録者

Martinez-Hackert, E.,Hendrickson, W.A. (登録日: 2010-11-29, 公開日: 2011-01-19, 最終更新日: 2024-02-21)

主引用文献

Martinez-Hackert, E.,Hendrickson, W.A.
Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26.
J.Mol.Biol., 407:450-464, 2011

PubMed Abstract: In the cell, protein folding is mediated by folding catalysts and chaperones. The two functions are often linked, especially when the catalytic module forms part of a multidomain protein, as in Methanococcus jannaschii peptidyl-prolyl cis/trans isomerase FKBP26. Here, we show that FKBP26 chaperone activity requires both a 50-residue insertion in the catalytic FKBP domain, also called 'Insert-in-Flap' or IF domain, and an 80-residue C-terminal domain. We determined FKBP26 structures from four crystal forms and analyzed chaperone domains in light of their ability to mediate protein-protein interactions. FKBP26 is a crescent-shaped homodimer. We reason that folding proteins are bound inside the large crescent cleft, thus enabling their access to inward-facing peptidyl-prolyl cis/trans isomerase catalytic sites and ipsilateral chaperone domain surfaces. As these chaperone surfaces participate extensively in crystal lattice contacts, we speculate that the observed lattice contacts reflect a proclivity for protein associations and represent substrate interactions by FKBP26 chaperone domains. Finally, we find that FKBP26 is an exceptionally flexible molecule, suggesting a mechanism for nonspecific substrate recognition.

PubMed: 21262232
DOI: 10.1016/j.jmb.2011.01.027

実験手法

X-RAY DIFFRACTION (2.2 Å)