3lip
From Proteopedia
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|PDB= 3lip |SIZE=350|CAPTION= <scene name='initialview01'>3lip</scene>, resolution 2.0Å | |PDB= 3lip |SIZE=350|CAPTION= <scene name='initialview01'>3lip</scene>, resolution 2.0Å | ||
|SITE= <scene name='pdbsite=ACT:Catalytic+Triad+Residues'>ACT</scene> and <scene name='pdbsite=OXY:Oxyanion+Hole'>OXY</scene> | |SITE= <scene name='pdbsite=ACT:Catalytic+Triad+Residues'>ACT</scene> and <scene name='pdbsite=OXY:Oxyanion+Hole'>OXY</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lip OCA], [http://www.ebi.ac.uk/pdbsum/3lip PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3lip RCSB]</span> | ||
}} | }} | ||
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[[Category: Lang, D A.]] | [[Category: Lang, D A.]] | ||
[[Category: Schomburg, D.]] | [[Category: Schomburg, D.]] | ||
| - | [[Category: CA]] | ||
[[Category: catalytic triad]] | [[Category: catalytic triad]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: without inhibitor]] | [[Category: without inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:34:19 2008'' |
Revision as of 02:34, 31 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OPEN CONFORMATION OF PSEUDOMONAS CEPACIA LIPASE
Overview
BACKGROUND:. The interfacial activation of lipases results primarily from conformational changes in the enzymes which expose the active site and provide a hydrophobic surface for interaction with the lipid substrate. Comparison of the crystallization conditions used and the structures observed for a variety of lipases suggests that the enzyme conformation is dependent on solution conditions. Pseudomonas cepacia lipase (PCL) was crystallized in conditions from which the open, active conformation of the enzyme was expected. Its three-dimensional structure was determined independently in three different laboratories and was compared with the previously reported closed conformations of the closely related lipases from Pseudomonas glumae (PGL) and Chromobacterium viscosum (CVL). These structures provide new insights into the function of this commercially important family of lipases. RESULTS:. The three independent structures of PCL superimpose with only small differences in the mainchain conformations. As expected, the observed conformation reveals a catalytic site exposed to the solvent. Superposition of PCL with the PGL and CVL structures indicates that the rearrangement from the closed to the open conformation involves three loops. The largest movement involves a 40 residue stretch, within which a helical segment moves to afford access to the catalytic site. A hydrophobic cleft that is presumed to be the lipid binding site is formed around the active site. CONCLUSIONS:. The interfacial activation of Pseudomonas lipases involves conformational rearrangements of surface loops and appears to conform to models of activation deduced from the structures of fungal and mammalian lipases. Factors controlling the conformational rearrangement are not understood, but a comparison of crystallization conditions and observed conformation suggests that the conformation of the protein is determined by the solution conditions, perhaps by the dielectric constant.
About this Structure
3LIP is a Single protein structure of sequence from Burkholderia cepacia. Full crystallographic information is available from OCA.
Reference
The open conformation of a Pseudomonas lipase., Schrag JD, Li Y, Cygler M, Lang D, Burgdorf T, Hecht HJ, Schmid R, Schomburg D, Rydel TJ, Oliver JD, Strickland LC, Dunaway CM, Larson SB, Day J, McPherson A, Structure. 1997 Feb 15;5(2):187-202. PMID:9032074
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