8P3A
bacteriophage T5 l-alanoyl-d-glutamate peptidase Zn2+/Ca2+ form
Summary for 8P3A
| Entry DOI | 10.2210/pdb8p3a/pdb |
| Related | 2MXZ 2VO9 |
| NMR Information | BMRB: 34817 |
| Descriptor | L-alanyl-D-glutamate peptidase, ZINC ION, CALCIUM ION (3 entities in total) |
| Functional Keywords | l-alanoyl-d-glutamate peptidase, bacteriophage t5, endolysin, zn2+ and ca2+ containing form, antimicrobial protein |
| Biological source | Escherichia phage T5 |
| Total number of polymer chains | 1 |
| Total formula weight | 15391.69 |
| Authors | Prokhorov, D.A.,Kutyshenko, V.P.,Mikoulinskaia, G.V. (deposition date: 2023-05-17, release date: 2023-07-05, Last modification date: 2025-01-15) |
| Primary citation | 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 Cited by 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: 37686055DOI: 10.3390/ijms241713249 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
