1tah: Difference between revisions

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{{STRUCTURE_1tah|  PDB=1tah  |  SCENE=  }}  
{{STRUCTURE_1tah|  PDB=1tah  |  SCENE=  }}  


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




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Johnson, L N.]]
[[Category: Johnson, L N.]]
[[Category: Noble, M E.M.]]
[[Category: Noble, M E.M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:21:45 2008''

Revision as of 17:21, 28 July 2008

File:1tah.png

Template:STRUCTURE 1tah

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

Template:ABSTRACT PUBMED 8405390

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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