Lipase lid morph

From Proteopedia

For an introduction to the structure and function of lipase, please see the article Lipase. This Lipase lid morph article is a supplement to the main article on Lipase.

Candida rugosa lipase (triacylglycerol hydrolase) has been observed in two conformations, with the "lid" (residues 66-92^[1]) closed (1trh) or open (1lpm)^[1].

• Closed LID ().
• LID with inhibitor (1R)-menthyl hexyl phosphonate (C O P).

A morph^[2] shows the lid opening and closing.

• (LID).
• (LID, catalytic triad: Ser209, Glu341, and His449^[1]).
  

When the lid is closed, the enzyme surface is largely Polar. When the lid opens, a Hydrophobic pocket is exposed with the catalytic triad in the bottom.

• (Polar, Hydrophobic, catalytic triad: Ser209, Glu341, and His449^[1]).

An alternate morph^[3] shows a different path between the . The position of the inhibitor in the 1lpm structure is shown throughout; it would clash with the conformation of the lid in the 1trh structures, showing that closed lid and inhibitor binding are mutually exclusive.

See Also

• Lipase, the main article in Proteopedia.
• Molecular Playground/Pancreatic Lipase
• Lipase in Wikipedia

Notes and References

1. ↑ ^{1.0 1.1 1.2 1.3} Grochulski P, Li Y, Schrag JD, Cygler M. Two conformational states of Candida rugosa lipase. Protein Sci. 1994 Jan;3(1):82-91. PMID:8142901
2. ↑ This is a linear interpolation morph. The 14-model PDB file is Image:Morph-linear-1trh-1lpm.pdb.gz.
3. ↑ This is a rigid body morph based on the superposition in PDB file Image:1TRH 1LPM.pdb. It is created by the Storymorph script on the fly.