4MSP

Crystal structure of human peptidyl-prolyl cis-trans isomerase FKBP22 (aka FKBP14) containing two EF-hand motifs

4MSP の概要

• エントリーDOI: 10.2210/pdb4msp/pdb
• 分子名称: Peptidyl-prolyl cis-trans isomerase FKBP14, CALCIUM ION, PENTAETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: fkbp-type domain, ef-hand motif, peptidyl-prolyl cis-trans isomerase, calcium binding, endoplasmic reticulum, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endoplasmic reticulum lumen : Q9NWM8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47051.69

構造登録者

Boudko, S.P.,Ishikawa, Y.,Bachinger, H.P. (登録日: 2013-09-18, 公開日: 2013-12-25, 最終更新日: 2024-11-20)

主引用文献

Boudko, S.P.,Ishikawa, Y.,Nix, J.,Chapman, M.S.,Bachinger, H.P.
Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs.
Protein Sci., 23:67-75, 2014

PubMed Abstract: The FK506-binding protein (FKBP) family consists of proteins with a variety of protein-protein interaction domains and versatile cellular functions. It is assumed that all members are peptidyl-prolyl cis-trans isomerases with the enzymatic function attributed to the FKBP domain. Six members of this family localize to the mammalian endoplasmic reticulum (ER). Four of them, FKBP22 (encoded by the FKBP14 gene), FKBP23 (FKBP7), FKBP60 (FKBP9), and FKBP65 (FKBP10), are unique among all FKBPs as they contain the EF-hand motifs. Little is known about the biological roles of these proteins, but emerging genetics studies are attracting great interest to the ER resident FKBPs, as mutations in genes encoding FKBP10 and FKBP14 were shown to cause a variety of matrix disorders. Although the structural organization of the FKBP-type domain as well as of the EF-hand motif has been known for a while, it is difficult to conclude how these structures are combined and how it affects the protein functionality. We have determined a unique 1.9 Å resolution crystal structure for human FKBP22, which can serve as a prototype for other EF hand-containing FKBPs. The EF-hand motifs of two FKBP22 molecules form a dimeric complex with an elongated and predominantly hydrophobic cavity that can potentially be occupied by an aliphatic ligand. The FKBP-type domains are separated by a cleft and their putative active sites can catalyze isomerazation of two bonds within a polypeptide chain in extended conformation. These structural results are of prime interest for understanding biological functions of ER resident FKBPs containing EF-hand motifs.

PubMed: 24272907
DOI: 10.1002/pro.2391

実験手法

X-RAY DIFFRACTION (1.9 Å)