1gpl
From Proteopedia
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| - | [[Image:1gpl.gif|left|200px]] | + | [[Image:1gpl.gif|left|200px]] |
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| - | '''RP2 LIPASE''' | + | {{Structure |
| + | |PDB= 1gpl |SIZE=350|CAPTION= <scene name='initialview01'>1gpl</scene>, resolution 2.01Å | ||
| + | |SITE= <scene name='pdbsite=CAT:Catalytic+Triad.+The+Nucleophile+SER+152+Is+Located+In+A+...'>CAT</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''RP2 LIPASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GPL is a [ | + | 1GPL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPL OCA]. |
==Reference== | ==Reference== | ||
| - | Pancreatic lipase structure-function relationships by domain exchange., Carriere F, Thirstrup K, Hjorth S, Ferrato F, Nielsen PF, Withers-Martinez C, Cambillau C, Boel E, Thim L, Verger R, Biochemistry. 1997 Jan 7;36(1):239-48. PMID:[http:// | + | Pancreatic lipase structure-function relationships by domain exchange., Carriere F, Thirstrup K, Hjorth S, Ferrato F, Nielsen PF, Withers-Martinez C, Cambillau C, Boel E, Thim L, Verger R, Biochemistry. 1997 Jan 7;36(1):239-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8993339 8993339] |
[[Category: Cavia porcellus]] | [[Category: Cavia porcellus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: lipid degradation]] | [[Category: lipid degradation]] | ||
| - | [[Category: | + | [[Category: pancrea]] |
[[Category: serine esterase]] | [[Category: serine 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 11:26:15 2008'' |
Revision as of 09:26, 20 March 2008
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| , resolution 2.01Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RP2 LIPASE
Contents |
Overview
We designed chimeric mutants by exchanging the lid domains of the classical human pancreatic lipase (HPL) and the guinea pig pancreatic lipase related protein 2 (GPLRP2). This latter enzyme possesses naturally a large deletion within the lid domain and is not activated by lipid/water interfaces. Furthermore, GPLRP2 exhibits phospholipase A1 and lipase activities in the same order of magnitude, whereas HPL has no significant phospholipase activity and displays a clear interfacial activation. An HPL mutant [HPL(-lid)] with GPLRP2 mini-lid domain does not display interfacial activation. Its specific activity toward triglycerides is, however, dramatically reduced. A GPLRP2 mutant [GPLRP2(+lid)] with HPL full-length lid domain is not interfacially activated, and its lid domain probably exists under a permanent open conformation. Therefore, the phenomenon of interfacial activation in HPL is not only due to the presence of a full-length lid domain but also to other structural elements which probably allow the existence of stabilized closed and open conformations of the lid. GPLRP2(+lid) phospholipase activity is significantly reduced as compared to GPLRP2, whereas its lipase activity remains at the same level. Therefore, the lid domain plays a major role in substrate selectivity and can be considered as part of the active site. However, the presence of a full-length lid domain is not sufficient to explain the absence of phospholipase activity in HPL since HPL(-lid) does not display any phospholipase activity. We also produced a chimeric GPLRP2 mutant in which the C-terminal domain was substituted by the HPL C-terminal domain. The colipase effects, i.e., anchoring and stabilization of the lipase at the interface, are clearly observed with the chimera, whereas GPLRP2 is insensitive to colipase. The kinetic characterization of this chimera reveals for the first time that the interfacial stability of pancreatic lipases depends on the structure of the C-terminal domain.
Disease
Known disease associated with this structure: Pancreatic lipase deficiency OMIM:[246600]
About this Structure
1GPL is a Single protein structure of sequence from Cavia porcellus. Full crystallographic information is available from OCA.
Reference
Pancreatic lipase structure-function relationships by domain exchange., Carriere F, Thirstrup K, Hjorth S, Ferrato F, Nielsen PF, Withers-Martinez C, Cambillau C, Boel E, Thim L, Verger R, Biochemistry. 1997 Jan 7;36(1):239-48. PMID:8993339
Page seeded by OCA on Thu Mar 20 11:26:15 2008
