4ODR

Structure of SlyD delta-IF from Thermus thermophilus in complex with FK506

4ODR の概要

• エントリーDOI: 10.2210/pdb4odr/pdb
• 関連するPDBエントリー: 4ODK 4ODL 4ODM 4ODN 4ODO 4ODP 4ODQ
• 分子名称: Peptidyl-prolyl cis-trans isomerase SlyD, Peptidyl-prolyl cis-trans isomerase FKBP1A chimera, 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN, ZINC ION, ... (7 entities in total)
• 機能のキーワード: fkbp domain, chaperone, peptidyl-prolyl isomerase, ppiase, isomerase
• 由来する生物種: Thermus thermophilus (bacteria, human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26963.96

構造登録者

Quistgaard, E.M.,Low, C.,Nordlund, P. (登録日: 2014-01-10, 公開日: 2015-01-14, 最終更新日: 2024-02-28)

主引用文献

Quistgaard, E.M.,Weininger, U.,Ural-Blimke, Y.,Modig, K.,Nordlund, P.,Akke, M.,Low, C.
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.
BMC Biol., 14:82-82, 2016

PubMed Abstract: Peptidyl-prolyl isomerases (PPIases) catalyze cis/trans isomerization of peptidyl-prolyl bonds, which is often rate-limiting for protein folding. SlyD is a two-domain enzyme containing both a PPIase FK506-binding protein (FKBP) domain and an insert-in-flap (IF) chaperone domain. To date, the interactions of these domains with unfolded proteins have remained rather obscure, with structural information on binding to the FKBP domain being limited to complexes involving various inhibitor compounds or a chemically modified tetrapeptide.

PubMed: 27664121
DOI: 10.1186/s12915-016-0300-3

実験手法

X-RAY DIFFRACTION (1.929 Å)