Motion in Lipase [lip]

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Classification Known Fragment Motion, Hinge Mechanism [F-h-2]

Structures 1CLE Candida rugoas cholesterol esterase [ PartsList ] 1CRL Candida rugoas lipase [ PartsList ] 1LPA Conformation 1 [ PartsList ] 1LPB Conformation 2 [ PartsList ] 1THG Otrichum candidum lipase [ PartsList ]

Description A number of lipases undergo an iterfacial activation. They bind their substrate at a lipid-water interface. They contain a lid which covers the active site when in solution, but is open at the interface to allow substrate binding. This has been show in at least two cases: human pancreatic lipase (1LPA, 1LPB) and candida rugoas lipase (1CRL), which have had their structures determined in the open and closed conformations. The same mechanism is also though to be important in the related structures Geotrichum candidum lipase (1TGH) and Candida rugosa cholesterol esterase (1CLE).

Particular values describing motion Creation Date = 19971130 Experimental Methods = x (Traditional x-ray) Modification Date = 1998-06-29 12:01:27.000

References Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D, Rubin B, Cygler M (1993). Insights into interfacial activation from an open structure of Candida rugosa lipase. J Biol Chem 268(17):12843-12847. [Medline info for 93286131] van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C (1993). Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature 362(6423):814-820. [Medline info for 93241293] van Tilbeurgh H, Sarda L, Verger R, Cambillau C (1992). Structure of the pancreatic lipase-procolipase complex. Nature 359(6391):159-162. [Medline info for 92396238]

GO terms associated with structures Molecular function enzyme activator activity, catalytic activity, triacylglycerol lipase activity Cellular component extracellular region Biological process lipid metabolism, digestion, lipid catabolism

Morphs

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Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu