4BF8

Fpr4 PPI domain

4BF8 の概要

• エントリーDOI: 10.2210/pdb4bf8/pdb
• NMR情報: BMRB: 17713
• 分子名称: FPR4 (1 entity in total)
• 機能のキーワード: isomerase, proline isomerization, fkbp, histone chaperone
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Nucleus : Q06205
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12502.85

構造登録者

Monneau, Y.,Mackereth, C. (登録日: 2013-03-15, 公開日: 2013-07-31, 最終更新日: 2024-06-19)

主引用文献

Monneau, Y.R.,Soufari, H.,Nelson, C.J.,Mackereth, C.D.
Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 Towards Histone H3 Proline Isomerization
J.Biol.Chem., 288:25826-, 2013

PubMed Abstract: The FK506-binding protein (FKBP) family of peptidyl-prolyl isomerases (PPIases) is characterized by a common catalytic domain that binds to the inhibitors FK506 and rapamycin. As one of four FKBPs within the yeast Saccharomyces cerevisiae, Fpr4 has been described as a histone chaperone, and is in addition implicated in epigenetic function in part due to its mediation of cis-trans conversion of proline residues within histone tails. To better understand the molecular details of this activity, we have determined the solution structure of the Fpr4 C-terminal PPIase domain by using NMR spectroscopy. This canonical FKBP domain actively increases the rate of isomerization of three decapeptides derived from the N terminus of yeast histone H3, whereas maintaining intrinsic cis and trans populations. Observation of the uncatalyzed and Fpr4-catalyzed isomerization rates at equilibrium demonstrate Pro(16) and Pro(30) of histone H3 as the major proline targets of Fpr4, with little activity shown against Pro(38). This alternate ranking of the three target prolines, as compared with affinity determination or the classical chymotrypsin-based fluorescent assay, reveals the mechanistic importance of substrate residues C-terminal to the peptidyl-prolyl bond.

PubMed: 23888048
DOI: 10.1074/JBC.M113.479964

実験手法

SOLUTION NMR