1tah
From Proteopedia
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| , resolution 3.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE
Overview
The family of lipases (triacylglycerol-acyl-hydrolases EC 3.1.1.3) constitutes an interesting class of enzymes because of their ability to interact with lipid-water interfaces, their wide range of substrate specificities, and their potential industrial applications. Here we report the first crystal structure of a bacterial lipase, from Pseudomonas glumae. The structure is formed from three domains, the largest of which contains a subset of the alpha/beta hydrolase fold and a calcium site. Asp263, the acidic residue in the catalytic triad, has previously been mutated into an alanine with only a modest reduction in activity.
About this Structure
1TAH is a Single protein structure of sequence from Burkholderia glumae. Full crystallographic information is available from OCA.
Reference
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate., Noble ME, Cleasby A, Johnson LN, Egmond MR, Frenken LG, FEBS Lett. 1993 Sep 27;331(1-2):123-8. PMID:8405390
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