5E4Y
Orthorhombic structure of the acetyl esterase MekB
Summary for 5E4Y
| Entry DOI | 10.2210/pdb5e4y/pdb |
| Descriptor | Homoserine O-acetyltransferase (2 entities in total) |
| Functional Keywords | esterase, alpha/beta hydrolase, methyl alkyl ketone degradation pathway, transferase, hydrolase |
| Biological source | Pseudomonas veronii |
| Total number of polymer chains | 2 |
| Total formula weight | 79493.88 |
| Authors | Niefind, K.,Toelzer, C.,Pal, S.,Watzlawick, H.,Altenbuchner, J. (deposition date: 2015-10-07, release date: 2015-12-16, Last modification date: 2024-01-10) |
| Primary citation | Tolzer, C.,Pal, S.,Watzlawick, H.,Altenbuchner, J.,Niefind, K. A novel esterase subfamily with alpha / beta-hydrolase fold suggested by structures of two bacterial enzymes homologous to l-homoserine O-acetyl transferases. Febs Lett., 590:174-184, 2016 Cited by PubMed Abstract: MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of α/β-hydrolase fold proteins. Based on sequence comparisons, they are annotated as homoserine transacetylases in popular databases like UNIPROT, PFAM or ESTHER. However, experimentally, MekB and CgHle were shown to be esterases that hydrolyse preferentially acetic acid esters. We describe the x-ray structures of these enzymes solved to high resolution. The overall structures confirm the close relatedness to experimentally validated homoserine acetyl transferases, but simultaneously the structures exclude the ability of MekB and CgHle to bind homoserine and acetyl-CoA. Insofar the MekB and CgHle structures suggest dividing the homoserine transacetylase family into subfamilies, namely genuine acetyl transferases and acetyl esterases with MekB and CgHle as constituting members of the latter. PubMed: 26787467DOI: 10.1002/1873-3468.12031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report
