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| | {{STRUCTURE_1hpl| PDB=1hpl | SCENE= }} | | {{STRUCTURE_1hpl| PDB=1hpl | SCENE= }} |
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| - | '''HORSE PANCREATIC LIPASE. THE CRYSTAL STRUCTURE AT 2.3 ANGSTROMS RESOLUTION'''
| + | ===HORSE PANCREATIC LIPASE. THE CRYSTAL STRUCTURE AT 2.3 ANGSTROMS RESOLUTION=== |
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| - | ==Overview==
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| - | Pancreatic lipase (EC 3.1.1.3) plays a key role in dietary fat digestion by converting triacylglycerols into 2-monoacylglycerols and free fatty acids in the intestine. Although the crystallographic structures of the human pancreatic lipase and of a human lipase-porcine colipase complex have been solved, no refined structure of pancreatic lipase has yet been published. The crystal structure of the horse enzyme was solved by the molecular replacement method from the model of the human pancreatic lipase and subsequently refined to 2.3 A resolution. The final model contains two molecules of 449 amino acid residues each in the asymmetric unit, 705 well-defined water molecules and two calcium ions. The two molecules in the asymmetric unit of the orthorhombic crystals are related by a 2-fold non-crystallographic symmetry axis as in the case of the human lipase. However, the association between the two molecules in their respective crystal forms is different. The overall molecular structure of the horse lipase is very similar to that of the human enzyme. The horse lipase is made up of two well-defined domains. The N-terminal domain which bears the active centre has a typical alpha/beta hydrolase fold topology. The C-terminal domain which is devoted to colipase binding has a beta-sheet sandwich topology. Comparison of equivalent C alpha atom positions between the final model of the horse lipase and the human lipase structure shows only slight differences which are mainly located in the C-terminal domain. The horse enzyme possesses the common features of the known mammalian and microbial lipases, in particular the "flap" covering the catalytic triad. In addition to more precise information concerning these features, the elucidation of the horse lipase crystal structure allowed us to better understand the structural basis of the kinetic behaviour of pancreatic lipases towards a soluble substrate, p-nitrophenyl acetate, and the different sensitivity of these enzymes towards limited proteolysis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8182745}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8182745 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8182745}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Bourne, Y.]] | | [[Category: Bourne, Y.]] |
| | [[Category: Cambillau, C.]] | | [[Category: Cambillau, C.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:05:51 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:30:32 2008'' |
Revision as of 05:30, 1 July 2008
Template:STRUCTURE 1hpl
HORSE PANCREATIC LIPASE. THE CRYSTAL STRUCTURE AT 2.3 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 8182745
About this Structure
1HPL is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
Horse pancreatic lipase. The crystal structure refined at 2.3 A resolution., Bourne Y, Martinez C, Kerfelec B, Lombardo D, Chapus C, Cambillau C, J Mol Biol. 1994 May 20;238(5):709-32. PMID:8182745
Page seeded by OCA on Tue Jul 1 08:30:32 2008
