1tia

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|SITE=
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|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]
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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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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tia OCA], [http://www.ebi.ac.uk/pdbsum/1tia PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tia RCSB]</span>
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[[Category: hydrolase(carboxylic esterase)]]
[[Category: hydrolase(carboxylic esterase)]]
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Revision as of 20:56, 30 March 2008


PDB ID 1tia

Drag the structure with the mouse to rotate
, resolution 2.1Å
Activity: Triacylglycerol lipase, with EC number 3.1.1.3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES


Overview

The stability of globular proteins arises largely from the burial of non-polar amino acids in their interior. These residues are efficiently packed to eliminate energetically unfavorable cavities. Contrary to these observations, high resolution X-ray crystallographic analyses of four homologous lipases from filamentous fungi reveal an alpha/beta fold which contains a buried conserved constellation of charged and polar side chains with associated cavities containing ordered water molecules. It is possible that this structural arrangement plays an important role in interfacial catalysis.

About this Structure

1TIA is a Single protein structure of sequence from Penicillium camemberti. Full crystallographic information is available from OCA.

Reference

An unusual buried polar cluster in a family of fungal lipases., Derewenda U, Swenson L, Green R, Wei Y, Dodson GG, Yamaguchi S, Haas MJ, Derewenda ZS, Nat Struct Biol. 1994 Jan;1(1):36-47. PMID:7656005

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