5MGX

The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90

5MGX の概要

• エントリーDOI: 10.2210/pdb5mgx/pdb
• 分子名称: yeast HSP90 C-terminus, Peptidyl-prolyl cis-trans isomerase FKBP8 (3 entities in total)
• 機能のキーワード: hsp90, ppiase, teratricopeptide, immunophilin, isomerase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Mitochondrion . Isoform 1: Mitochondrion membrane ; Single-pass membrane protein; Cytoplasmic side . Isoform 3: Mitochondrion membrane ; Single-pass membrane protein; Cytoplasmic side : Q14318
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 131086.60

構造登録者

Roe, S.M.,Blundell, K.L.,Prodromou, C. (登録日: 2016-11-22, 公開日: 2017-03-22, 最終更新日: 2024-01-17)

主引用文献

Blundell, K.L.,Pal, M.,Roe, S.M.,Pearl, L.H.,Prodromou, C.
The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90.
PLoS ONE, 12:e0173543-e0173543, 2017

PubMed Abstract: Tetratricopeptide (TPR) domains are known protein interaction domains. We show that the TPR domain of FKBP8 selectively binds Hsp90, and interactions upstream of the conserved MEEVD motif are critical for tight binding. In contrast FKBP8 failed to bind intact Hsp70. The PPIase domain was not essential for the interaction with Hsp90 and binding was completely encompassed by the TPR domain alone. The conformation adopted by Hsp90 peptides, containing the conserved MEEVD motif, in the crystal structure were similar to that seen for the TPR domains of CHIP, AIP and Tah1. The carboxylate clamp interactions with bound Hsp90 peptide were a critical component of the interaction and mutation of Lys 307, involved in the carboxylate clamp, completely disrupted the interaction with Hsp90. FKBP8 binding to Hsp90 did not substantially influence its ATPase activity.

PubMed: 28278223
DOI: 10.1371/journal.pone.0173543

実験手法

X-RAY DIFFRACTION (2.18 Å)