From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2lip.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2lip.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2lip| PDB=2lip | SCENE= }} | | {{STRUCTURE_2lip| PDB=2lip | SCENE= }} |
| | | | |
| - | '''PSEUDOMONAS LIPASE OPEN CONFORMATION'''
| + | ===PSEUDOMONAS LIPASE OPEN CONFORMATION=== |
| | | | |
| | | | |
| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9032074}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9032074 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9032074}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Lipase]] | | [[Category: Lipase]] |
| | [[Category: Pseudomona]] | | [[Category: Pseudomona]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:30:52 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:12:33 2008'' |
Revision as of 04:12, 28 July 2008
Template:STRUCTURE 2lip
PSEUDOMONAS LIPASE OPEN CONFORMATION
Template:ABSTRACT PUBMED 9032074
About this Structure
2LIP 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
Page seeded by OCA on Mon Jul 28 07:12:33 2008
