Lipase lid morph

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Candida rugosa lipase (1trh, 1lpm).

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

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.

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