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 functioncatalytic activity, triacylglycerol lipase activity, enzyme activator activity
Cellular componentextracellular region
Biological processlipid catabolism, lipid metabolism, digestion

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
593692-25810 Human lipase 1lpa [ B ] 1eth [ A ] 448
24279-21107 Lipase 1lpa [ A ] 1lpb [ A ] 95
602859-28187 Lipase 1crl [ A ] 1thg [ A ] 543
603880-29889 Lipase 1crl [ A ] 1thg [ A ] 543
425655-24077 Lipase 1tgl [ A ] 4tgl [ A ] 269
35371-26618 Via_align 1lpa [ A ] 1lpb [ A ] 95

Automatic morphs
Morph Morph name Structure #1 Structure #2 Residues
va1dt3B-1einB Lipase 1dt3 [ B ] 1ein [ B ] 269
va1einA-1dt3B Lipase 1ein [ A ] 1dt3 [ B ] 269
va1einC-1dt3B Lipase 1ein [ C ] 1dt3 [ B ] 269
va1dt3B-1dteB Lipase 1dt3 [ B ] 1dte [ B ] 269
va1dt3B-1dteA Lipase 1dt3 [ B ] 1dte [ A ] 269
va1einB-1dt3A Lipase 1ein [ B ] 1dt3 [ A ] 269
va1einA-1dt3A Lipase 1ein [ A ] 1dt3 [ A ] 269
va1einC-1dt3A Lipase 1ein [ C ] 1dt3 [ A ] 269
va1dt3A-1dteB Lipase 1dt3 [ A ] 1dte [ B ] 269
va1einB-1dt5E Lipase 1ein [ B ] 1dt5 [ E ] 269
va1einB-1dt5G Lipase 1ein [ B ] 1dt5 [ G ] 269
va1einA-1dt5E Lipase 1ein [ A ] 1dt5 [ E ] 269
va1dt5D-1einB Lipase 1dt5 [ D ] 1ein [ B ] 269
va1dt5B-1einB Lipase 1dt5 [ B ] 1ein [ B ] 269
va1einC-1dt5E Lipase 1ein [ C ] 1dt5 [ E ] 269
va1dteB-1tibA Lipase 1dte [ B ] 1tib [ A ] 269
va1einB-1dt5C Lipase 1ein [ B ] 1dt5 [ C ] 269
va1einA-1dt5G Lipase 1ein [ A ] 1dt5 [ G ] 269
va1einA-1dt5D Lipase 1ein [ A ] 1dt5 [ D ] 269
va1dt5H-1einB Lipase 1dt5 [ H ] 1ein [ B ] 269
va1einA-1dt5F Lipase 1ein [ A ] 1dt5 [ F ] 269
va1einC-1dt5B Lipase 1ein [ C ] 1dt5 [ B ] 269
va1einA-1dt5C Lipase 1ein [ A ] 1dt5 [ C ] 269
va1dteA-1tibA Lipase 1dte [ A ] 1tib [ A ] 269
va1einC-1dt5C Lipase 1ein [ C ] 1dt5 [ C ] 269
va1einC-1dt5H Lipase 1ein [ C ] 1dt5 [ H ] 269
va1du4C-1einC Lipase 1du4 [ C ] 1ein [ C ] 269
va1dt5A-1dteB Lipase 1dt5 [ A ] 1dte [ B ] 269
va1dt5E-1dteB Lipase 1dt5 [ E ] 1dte [ B ] 269
va1dt5G-1dteB Lipase 1dt5 [ G ] 1dte [ B ] 269
va1dt5F-1dteB Lipase 1dt5 [ F ] 1dte [ B ] 269
va1einA-1du4A Lipase 1ein [ A ] 1du4 [ A ] 269
va1dteA-1dt5G Lipase 1dte [ A ] 1dt5 [ G ] 269
va1du4D-1dteB Lipase 1du4 [ D ] 1dte [ B ] 269
va1dt5B-1dteA Lipase 1dt5 [ B ] 1dte [ A ] 269
va1dt5F-1dteA Lipase 1dt5 [ F ] 1dte [ A ] 269
va1dt5H-1dteA Lipase 1dt5 [ H ] 1dte [ A ] 269
va1du4C-1dteB Lipase 1du4 [ C ] 1dte [ B ] 269
va1du4B-1einB Lipase 1du4 [ B ] 1ein [ B ] 269
va1du4A-1dteB Lipase 1du4 [ A ] 1dte [ B ] 269
va1dteA-1du4A Lipase 1dte [ A ] 1du4 [ A ] 269
va1dteA-1dt3A Lipase 1dte [ A ] 1dt3 [ A ] 269
va1einB-1dt5A Lipase 1ein [ B ] 1dt5 [ A ] 269
va1einA-1dt5A Lipase 1ein [ A ] 1dt5 [ A ] 269
va1einC-1dt5A Lipase 1ein [ C ] 1dt5 [ A ] 269
va1dt5F-1einB Lipase 1dt5 [ F ] 1ein [ B ] 269
va1einA-1dt5B Lipase 1ein [ A ] 1dt5 [ B ] 269
va1einB-1du4D Lipase 1ein [ B ] 1du4 [ D ] 269
va1einC-1dt5G Lipase 1ein [ C ] 1dt5 [ G ] 269
va1einC-1dt5D Lipase 1ein [ C ] 1dt5 [ D ] 269
va1einA-1du4D Lipase 1ein [ A ] 1du4 [ D ] 269
va1einC-1dt5F Lipase 1ein [ C ] 1dt5 [ F ] 269
va1einA-1dt5H Lipase 1ein [ A ] 1dt5 [ H ] 269
va1einC-1du4D Lipase 1ein [ C ] 1du4 [ D ] 269
va1du4C-1einB Lipase 1du4 [ C ] 1ein [ B ] 269
va1einA-1du4C Lipase 1ein [ A ] 1du4 [ C ] 269
va1einB-1du4A Lipase 1ein [ B ] 1du4 [ A ] 269
va1dt5B-1dteB Lipase 1dt5 [ B ] 1dte [ B ] 269
va1dt5D-1dteB Lipase 1dt5 [ D ] 1dte [ B ] 269
va1dteA-1dt5E Lipase 1dte [ A ] 1dt5 [ E ] 269
va1dteA-1dt5A Lipase 1dte [ A ] 1dt5 [ A ] 269
va1dt5C-1dteB Lipase 1dt5 [ C ] 1dte [ B ] 269
va1dt5H-1dteB Lipase 1dt5 [ H ] 1dte [ B ] 269
va1einC-1du4A Lipase 1ein [ C ] 1du4 [ A ] 269
va1dt5D-1dteA Lipase 1dt5 [ D ] 1dte [ A ] 269
va1dteA-1dt5C Lipase 1dte [ A ] 1dt5 [ C ] 269
va1du4D-1dteA Lipase 1du4 [ D ] 1dte [ A ] 269
va1dteA-1du4C Lipase 1dte [ A ] 1du4 [ C ] 269
va1einA-1du4B Lipase 1ein [ A ] 1du4 [ B ] 269
va1einC-1du4B Lipase 1ein [ C ] 1du4 [ B ] 269
va1crlA-1trhA Lipase (E.C. 3.1.1.3) (Triacyl 1crl [ A ] 1trh [ A ] 534
va1tibA-1einB Lipase (E.C. 3.1.1.3) (Triacyl 1tib [ A ] 1ein [ B ] 269
va1tibA-1einA Lipase (E.C. 3.1.1.3) (Triacyl 1tib [ A ] 1ein [ A ] 269
va1tibA-1einC 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