8P3A

bacteriophage T5 l-alanoyl-d-glutamate peptidase Zn2+/Ca2+ form

8P3A の概要

• エントリーDOI: 10.2210/pdb8p3a/pdb
• 関連するPDBエントリー: 2MXZ 2VO9
• NMR情報: BMRB: 34817
• 分子名称: L-alanyl-D-glutamate peptidase, ZINC ION, CALCIUM ION (3 entities in total)
• 機能のキーワード: l-alanoyl-d-glutamate peptidase, bacteriophage t5, endolysin, zn2+ and ca2+ containing form, antimicrobial protein
• 由来する生物種: Escherichia phage T5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15391.69

構造登録者

Prokhorov, D.A.,Kutyshenko, V.P.,Mikoulinskaia, G.V. (登録日: 2023-05-17, 公開日: 2023-07-05, 最終更新日: 2025-01-15)

主引用文献

Mikoulinskaia, G.V.,Prokhorov, D.A.,Chernyshov, S.V.,Sitnikova, D.S.,Arakelian, A.G.,Uversky, V.N.
Conservative Tryptophan Residue in the Vicinity of an Active Site of the M15 Family l,d-Peptidases: A Key Element in the Catalysis.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: Bioinformatics analysis of the sequences of orthologous zinc-containing peptidases of the M15_C subfamily revealed the presence of a conserved tryptophan residue near the active site, which is not involved in the formation of the protein core. Site-directed mutagenesis of this Trp114/109 residue using two representatives of the family, l-alanoyl-d-glutamate peptidases of bacteriophages T5 (calcium-activated EndoT5) and RB49 (EndoRB49, without ion regulation) as examples, and further analysis of the H NMR spectra of the mutants showed that a decrease in the volume of the W → F → A residue leads to changes in the hydrophobic core and active center of the protein, and also decreases the affinity for regulatory Ca in the EndoT5 mutants. The inactive T5W114A mutant lacks the ability to bind the substrate. In general, the conserved Trp114/109 residue, due to the spatial restrictions of its side chain, significantly affects the formation of the catalytically active form of the enzyme and is critical for catalysis.

PubMed: 37686055
DOI: 10.3390/ijms241713249

実験手法

SOLUTION NMR