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) closed (1trh) or open (1lpm).
- Closed LID ().
- LID with inhibitor (1R)-menthyl hexyl phosphonate (C O P).
A morph shows the lid opening and closing.
- (LID, catalytic triad: Ser209, Glu341, and His449).
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).
Notes and References
- ↑ 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
- ↑ This is a linear interpolation morph. The 14-model PDB file is Image:Morph-linear-1trh-1lpm.pdb.gz.