5EFZ

Monoclinic structure of the acetyl esterase MekB

Summary for 5EFZ

• Entry DOI: 10.2210/pdb5efz/pdb
• Related: 5E4Y
• Descriptor: Homoserine O-acetyltransferase, 1,2-ETHANEDIOL, GLYCEROL, ... (5 entities in total)
• Functional Keywords: alpha/beta hydrolase, acetyl ester hydrolase, pseudomonas veronii, transferase, hydrolase
• Biological source: Pseudomonas veronii
• Total number of polymer chains: 6
• Total formula weight: 241183.39

Authors

Toelzer, C.,Pal, S.,Watzlawick, H.,Altenbuchner, J.,Niefind, K. (deposition date: 2015-10-26, release date: 2015-12-16, Last modification date: 2024-05-08)

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

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: 26787467
DOI: 10.1002/1873-3468.12031

Experimental method

X-RAY DIFFRACTION (1.82 Å)