1tah

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[[Image:1tah.gif|left|200px]]
[[Image:1tah.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1tah |SIZE=350|CAPTION= <scene name='initialview01'>1tah</scene>, resolution 3.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1tah", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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{{STRUCTURE_1tah| PDB=1tah | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tah OCA], [http://www.ebi.ac.uk/pdbsum/1tah PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tah RCSB]</span>
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}}
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'''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'''
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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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[[Category: hydrolase(carboxylic esterase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:44:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:53:40 2008''
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Revision as of 06:44, 3 May 2008

Image:1tah.gif

Template:STRUCTURE 1tah

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 Page seeded by OCA on Sat May 3 09:44:29 2008

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