1tah: Difference between revisions
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[[Image:1tah.gif|left|200px]] | [[Image:1tah.gif|left|200px]] | ||
'''THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE''' | {{Structure | ||
|PDB= 1tah |SIZE=350|CAPTION= <scene name='initialview01'>1tah</scene>, resolution 3.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] | |||
|GENE= | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TAH is a [ | 1TAH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAH OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8405390 8405390] | ||
[[Category: Burkholderia glumae]] | [[Category: Burkholderia glumae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase(carboxylic esterase)]] | [[Category: hydrolase(carboxylic esterase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:15:58 2008'' | ||
Revision as of 12:15, 20 March 2008
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| 1tah, resolution 3.0Å | |||||||||||||
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| Ligands: | CA | ||||||||||||
| 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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