1TAH

THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE

Summary for 1TAH

• Entry DOI: 10.2210/pdb1tah/pdb
• Descriptor: LIPASE, CALCIUM ION (2 entities in total)
• Functional Keywords: hydrolase(carboxylic esterase)
• Biological source: Burkholderia glumae
• Cellular location: Secreted : Q05489
• Total number of polymer chains: 4
• Total formula weight: 132346.81

Authors

Noble, M.E.M.,Cleasby, A.,Johnson, L.N.,Egmond, M.,Frenken, L.G.J. (deposition date: 1993-12-21, release date: 1994-05-31, Last modification date: 2024-11-20)

Primary citation

Noble, M.E.,Cleasby, A.,Johnson, L.N.,Egmond, M.R.,Frenken, L.G.
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate.
FEBS Lett., 331:123-128, 1993

PubMed Abstract: 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.

PubMed: 8405390
DOI: 10.1016/0014-5793(93)80310-Q

Experimental method

X-RAY DIFFRACTION (3 Å)