5Z01
Native Escherichia coli L,D-carboxypeptidase A (LdcA)
Summary for 5Z01
| Entry DOI | 10.2210/pdb5z01/pdb |
| Descriptor | Murein tetrapeptide carboxypeptidase, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | peptidoglycan, recycling, cell-wall, hydrolase |
| Biological source | Escherichia coli (strain K12) |
| Cellular location | Cytoplasm : P76008 |
| Total number of polymer chains | 1 |
| Total formula weight | 35711.95 |
| Authors | Meyer, K.,Tame, J.R.H. (deposition date: 2017-12-18, release date: 2018-04-25, Last modification date: 2024-03-27) |
| Primary citation | Meyer, K.,Addy, C.,Akashi, S.,Roper, D.I.,Tame, J.R.H. The crystal structure and oligomeric form of Escherichia colil,d-carboxypeptidase A. Biochem. Biophys. Res. Commun., 499:594-599, 2018 Cited by PubMed Abstract: Bacterial peptidoglycan is constructed by cross-linking sugar chains carrying pentapeptide building blocks with two d-alanine residues at the C-terminus. Incorporation into the polymer and subsequent breakdown of peptidoglycan releases a tetrapeptide with a single d-alanine residue. Removal of this residue is necessary for the tripeptide to receive a new D-Ala-D-Ala dipeptide in the synthetic pathway, but proteases are generally unable to work with substrates having residues of unusual chirality close to the scissile bond. Processing of the tetrapeptide is carried out by a dedicated ld-carboxypeptidase, which is of interest as a novel drug target. We describe the high resolution crystal structure of the enzyme from E. coli, and demonstrate the dimeric structure is highly conserved. PubMed: 29601819DOI: 10.1016/j.bbrc.2018.03.195 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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