Summary for 1J3G
| Entry DOI | 10.2210/pdb1j3g/pdb |
| Descriptor | AmpD protein, ZINC ION (2 entities in total) |
| Functional Keywords | mixed alpha-beta, hydrolase |
| Biological source | Citrobacter freundii |
| Cellular location | Cytoplasm (By similarity): P82974 |
| Total number of polymer chains | 1 |
| Total formula weight | 20936.77 |
| Authors | Liepinsh, E.,Genereux, C.,Dehareng, D.,Joris, B.,Otting, G. (deposition date: 2003-01-31, release date: 2003-02-18, Last modification date: 2023-12-27) |
| Primary citation | Liepinsh, E.,Genereux, C.,Dehareng, D.,Joris, B.,Otting, G. NMR Structure of Citrobacter freundii AmpD, Comparison with Bacteriophage T7 Lysozyme and Homology with PGRP Domains J.Mol.Biol., 327:833-842, 2003 Cited by PubMed Abstract: AmpD is a bacterial amidase involved in the recycling of cell-wall fragments in Gram-negative bacteria. Inactivation of AmpD leads to derepression of beta-lactamase expression, presenting a major pathway for the acquisition of constitutive antibiotic resistance. Here, we report the NMR structure of AmpD from Citrobacter freundii (PDB accession code 1J3G). A deep substrate-binding pocket explains the observed specificity for low molecular mass substrates. The fold is related to that of bacteriophage T7 lysozyme. Both proteins bind zinc at a conserved site and require zinc for amidase activity, although the enzymatic mechanism seems to differ in detail. The structure-based sequence alignment identifies conserved features that are also conserved in the eukaryotic peptidoglycan recognition protein (PGRP) domains, including the zinc-coordination site in several of them. PGRP domains thus belong to the same fold family and, where zinc-binding residues are conserved, may have amidase activity. This hypothesis is supported by the observation that human serum N-acetylmuramyl-L-alanine amidase seems to be identical with a soluble form of human PGRP-L. PubMed: 12654266DOI: 10.1016/S0022-2836(03)00185-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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