6GMG

Structure of a glutamine donor mimicking inhibitory peptide shaped by the catalytic cleft of microbial transglutaminase

6GMG の概要

• エントリーDOI: 10.2210/pdb6gmg/pdb
• 分子名称: PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE, Papain inhibitor, CITRATE ANION, ... (5 entities in total)
• 機能のキーワード: transglutaminase ; streptomyces mobaraensis ; peptidic inhibitors; enzyme peptide interaction, transferase
• 由来する生物種: Streptomyces mobaraensis NBRC 13819 = DSM 40847; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78564.88

構造登録者

Schmelz, S.,Juettner, N.E.,Fuchsbauer, H.L.,Scrima, A. (登録日: 2018-05-25, 公開日: 2018-10-24, 最終更新日: 2024-11-06)

主引用文献

Juettner, N.E.,Schmelz, S.,Kraemer, A.,Knapp, S.,Becker, B.,Kolmar, H.,Scrima, A.,Fuchsbauer, H.L.
Structure of a glutamine donor mimicking inhibitory peptide shaped by the catalytic cleft of microbial transglutaminase.
FEBS J., 285:4684-4694, 2018

PubMed Abstract: The protein cross-linking enzyme transglutaminase from Streptomyces mobaraensis (MTG) is frequently used to modify therapeutic proteins. In order to reveal the binding mode of glutamine donor substrates, we have now crystallized MTG covalently linked to large inhibitory peptides. A series of peptide structures were examined but DIPIGSKMTG, which was chloroacetylated at serine, was the only inhibitory molecule that resulted in an interpretable density map. We found that, besides the warhead (modified Ser6), Ile4 and Gly5 of the inhibitory peptide occupy the tight but extended hydrophobic bottom of the MTG-binding cleft. Both termini of the peptide protrude along the cleft walls almost perpendicular to the bottom of the extended cleft. This peptide model suggests a zipper-like cross-linking mechanism of self-assembled substrate proteins by MTG.

PubMed: 30318745
DOI: 10.1111/febs.14678

実験手法

X-RAY DIFFRACTION (2.25 Å)