Sandbox UC 9

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Contents 1 Title 1.1 subtitle 2 See Also 3 Notes and References

Title

subtitle

spinqualitylabelsall models Candida rugosa lipase (1trh, 1lpm). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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]).

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.