5D6O: Orthorhombic Crystal Structure Of An Acetylester Hydrolase From Corynebacterium Glutamicum

MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of alpha/beta-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.
PDB ID: 5D6ODownload
MMDB ID: 134715
PDB Deposition Date: 2015/8/12
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 5D6O: dimeric; determined by author and by software (PISA)
Molecular Components in 5D6O
Label Count Molecule
Proteins (2 molecules)
Homoserine O-acetyltransferase
Molecule annotation
Chemicals (17 molecules)
* Click molecule labels to explore molecular sequence information.

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