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 functionenzyme activator activity, catalytic activity, triacylglycerol lipase activity
Cellular componentextracellular region
Biological processlipid metabolism, digestion, lipid catabolism

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Lipase 1crl [ A ] 1thg [ A ] 543

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
Human lipase 1lpa [ B ] 1eth [ A ] 448
Lipase 1lpa [ A ] 1lpb [ A ] 95
Lipase 1crl [ A ] 1thg [ A ] 543
Lipase 1crl [ A ] 1thg [ A ] 543
Lipase 1tgl [ A ] 4tgl [ A ] 269
Via_align 1lpa [ A ] 1lpb [ A ] 95

Automatic morphs
Morph Morph name Structure #1 Structure #2 Residues
Lipase 1dt3 [ B ] 1ein [ B ] 269
Lipase 1ein [ A ] 1dt3 [ B ] 269
Lipase 1ein [ C ] 1dt3 [ B ] 269
Lipase 1dt3 [ B ] 1dte [ B ] 269
Lipase 1dt3 [ B ] 1dte [ A ] 269
Lipase 1ein [ B ] 1dt3 [ A ] 269
Lipase 1ein [ A ] 1dt3 [ A ] 269
Lipase 1ein [ C ] 1dt3 [ A ] 269
Lipase 1dt3 [ A ] 1dte [ B ] 269
Lipase 1ein [ B ] 1dt5 [ E ] 269
Lipase 1ein [ B ] 1dt5 [ G ] 269
Lipase 1ein [ A ] 1dt5 [ E ] 269
Lipase 1dt5 [ D ] 1ein [ B ] 269
Lipase 1dt5 [ B ] 1ein [ B ] 269
Lipase 1ein [ C ] 1dt5 [ E ] 269
Lipase 1dte [ B ] 1tib [ A ] 269
Lipase 1ein [ B ] 1dt5 [ C ] 269
Lipase 1ein [ A ] 1dt5 [ G ] 269
Lipase 1ein [ A ] 1dt5 [ D ] 269
Lipase 1dt5 [ H ] 1ein [ B ] 269
Lipase 1ein [ A ] 1dt5 [ F ] 269
Lipase 1ein [ C ] 1dt5 [ B ] 269
Lipase 1ein [ A ] 1dt5 [ C ] 269
Lipase 1dte [ A ] 1tib [ A ] 269
Lipase 1ein [ C ] 1dt5 [ C ] 269
Lipase 1ein [ C ] 1dt5 [ H ] 269
Lipase 1du4 [ C ] 1ein [ C ] 269
Lipase 1dt5 [ A ] 1dte [ B ] 269
Lipase 1dt5 [ E ] 1dte [ B ] 269
Lipase 1dt5 [ G ] 1dte [ B ] 269
Lipase 1dt5 [ F ] 1dte [ B ] 269
Lipase 1ein [ A ] 1du4 [ A ] 269
Lipase 1dte [ A ] 1dt5 [ G ] 269
Lipase 1du4 [ D ] 1dte [ B ] 269
Lipase 1dt5 [ B ] 1dte [ A ] 269
Lipase 1dt5 [ F ] 1dte [ A ] 269
Lipase 1dt5 [ H ] 1dte [ A ] 269
Lipase 1du4 [ C ] 1dte [ B ] 269
Lipase 1du4 [ B ] 1ein [ B ] 269
Lipase 1du4 [ A ] 1dte [ B ] 269
Lipase 1dte [ A ] 1du4 [ A ] 269
Lipase 1dte [ A ] 1dt3 [ A ] 269
Lipase 1ein [ B ] 1dt5 [ A ] 269
Lipase 1ein [ A ] 1dt5 [ A ] 269
Lipase 1ein [ C ] 1dt5 [ A ] 269
Lipase 1dt5 [ F ] 1ein [ B ] 269
Lipase 1ein [ A ] 1dt5 [ B ] 269
Lipase 1ein [ B ] 1du4 [ D ] 269
Lipase 1ein [ C ] 1dt5 [ G ] 269
Lipase 1ein [ C ] 1dt5 [ D ] 269
Lipase 1ein [ A ] 1du4 [ D ] 269
Lipase 1ein [ C ] 1dt5 [ F ] 269
Lipase 1ein [ A ] 1dt5 [ H ] 269
Lipase 1ein [ C ] 1du4 [ D ] 269
Lipase 1du4 [ C ] 1ein [ B ] 269
Lipase 1ein [ A ] 1du4 [ C ] 269
Lipase 1ein [ B ] 1du4 [ A ] 269
Lipase 1dt5 [ B ] 1dte [ B ] 269
Lipase 1dt5 [ D ] 1dte [ B ] 269
Lipase 1dte [ A ] 1dt5 [ E ] 269
Lipase 1dte [ A ] 1dt5 [ A ] 269
Lipase 1dt5 [ C ] 1dte [ B ] 269
Lipase 1dt5 [ H ] 1dte [ B ] 269
Lipase 1ein [ C ] 1du4 [ A ] 269
Lipase 1dt5 [ D ] 1dte [ A ] 269
Lipase 1dte [ A ] 1dt5 [ C ] 269
Lipase 1du4 [ D ] 1dte [ A ] 269
Lipase 1dte [ A ] 1du4 [ C ] 269
Lipase 1ein [ A ] 1du4 [ B ] 269
Lipase 1ein [ C ] 1du4 [ B ] 269
Lipase (E.C. 3.1.1.3) (Triacyl 1crl [ A ] 1trh [ A ] 534
Lipase (E.C. 3.1.1.3) (Triacyl 1tib [ A ] 1ein [ B ] 269
Lipase (E.C. 3.1.1.3) (Triacyl 1tib [ A ] 1ein [ A ] 269
Lipase (E.C. 3.1.1.3) (Triacyl 1tib [ A ] 1ein [ C ] 269

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