4PA5

Tgl - a bacterial spore coat transglutaminase - cystamine complex

4PA5 の概要

• エントリーDOI: 10.2210/pdb4pa5/pdb
• 関連するPDBエントリー: 4P8I
• 分子名称: Protein-glutamine gamma-glutamyltransferase, TRIETHYLENE GLYCOL, 1,2-ETHANEDIOL, ... (10 entities in total)
• 機能のキーワード: protein cross-linking, baterial spore coat, nlpc/p60 endopeptidase, papain, transferase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61313.72

構造登録者

Brito, J.A.,Placido, D.,Fernandes, C.G.,Lousa, D.,Isidro, A.,Soares, C.M.,Pohl, J.,Carrondo, M.A.,Henriques, A.O.,Archer, M. (登録日: 2014-04-07, 公開日: 2015-09-30, 最終更新日: 2024-05-01)

主引用文献

Fernandes, C.G.,Placido, D.,Lousa, D.,Brito, J.A.,Isidro, A.,Soares, C.M.,Pohl, J.,Carrondo, M.A.,Archer, M.,Henriques, A.O.
Structural and Functional Characterization of an Ancient Bacterial Transglutaminase Sheds Light on the Minimal Requirements for Protein Cross-Linking.
Biochemistry, 54:5723-5734, 2015

PubMed Abstract: Transglutaminases are best known for their ability to catalyze protein cross-linking reactions that impart chemical and physical resilience to cellular structures. Here, we report the crystal structure and characterization of Tgl, a transglutaminase from the bacterium Bacillus subtilis. Tgl is produced during sporulation and cross-links the surface of the highly resilient spore. Tgl-like proteins are found only in spore-forming bacteria of the Bacillus and Clostridia classes, indicating an ancient origin. Tgl is a single-domain protein, produced in active form, and the smallest transglutaminase characterized to date. We show that Tgl is structurally similar to bacterial cell wall endopeptidases and has an NlpC/P60 catalytic core, thought to represent the ancestral unit of the cysteine protease fold. We show that Tgl functions through a unique partially redundant catalytic dyad formed by Cys116 and Glu187 or Glu115. Strikingly, the catalytic Cys is insulated within a hydrophobic tunnel that traverses the molecule from side to side. The lack of similarity of Tgl to other transglutaminases together with its small size suggests that an NlpC/P60 catalytic core and insulation of the active site during catalysis may be essential requirements for protein cross-linking.

PubMed: 26322858
DOI: 10.1021/acs.biochem.5b00661

実験手法

X-RAY DIFFRACTION (1.86 Å)