EC Number   |
Reference |
|---|
   2.3.2.B14 | 5,5'-dithio-bis-2-nitrobenzoic acid derivative, to 1.55 A resolution. The compound binds to the catalytic cysteine residue, Cys354, in both chains of the asymmetric unit |
756702 |
| 2.3.2.B14 | apo and faropenem-acylated forms of Ldt3 at 1.3 and 1.8 A resolution, respectively. The structures revealed a fold and catalytic diad similar to those of other Ldt enzymes. Docking of beta-lactam antibiotics at the active site suggests interaction with conserved amino acids. Faropenem may be degraded after Cys246 acylation, and possibly only a beta-hydroxybutanoate or an acetyl group covalently attached to the enzyme remains |
755696 |
| 2.3.2.B14 | crystal structures of L,D-transpeptidase 2 complexed with biapenem or tebipenem. Biapenem and tebipenem bind to the outer cavity, covalently inactivate the enzyme, and subsequently degrade via an S-conjugate elimination mechanism |
756285 |
| 2.3.2.B14 | hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 1 M succinic acid, and 1% (w/v) PEG MME 2000 |
721067 |
| 2.3.2.B14 | homology modeling and docking of faropenem and meropenem. In the LdtF-meropenem model, both hydrogens of the protonated secondary pyrrolidine nitrogen form a bidentate hydrogen bond with Asp353 |
755695 |
| 2.3.2.B14 | sitting drop vapour diffusion method |
675384 |
| 2.3.2.B14 | structure of L,D-transpeptidase 2 in the apo form and in complex with meropenem and imipenem. The periplasmic region of L,D-transpeptidase 2 folds into three domains. The catalytic residues are situated in the C-terminal domain. The acylation reaction occurs between carbapenem antibiotics and the catalytic Cys354 forming a covalent complex. This adduct formation mimics the acylation of L,D-transpeptidase 2 with the donor PG-stem. In the crystal structures of the apo and the carbapenem complexes, the N-terminal domain has a muropeptide unit non-covalently bound to it |
755669 |
| 2.3.2.B14 | structure of Ldt2 (fragment DELTAN41) at 2.98 A resolution and molecular dynamics simulations of complexes with cefdinir, cephalexin, doripenem, and tebipenem |
755806 |
| 2.3.2.B14 | structure of YcbB consists of a conserved L,D-transpeptidase catalytic domain decorated with a subdomain on the dynamic substrate capping loop, peptidoglycan-binding and large scaffolding domains. The YcbB-meropenem complex map has ordered density defining the active site residues including the thiol ester covalent link of Cys528 and acylated meropenem |
757743 |
