Lipase lid morph

From Proteopedia

Jump to: navigation, search

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]).

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

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.

Proteopedia Page Contributors and Editors (what is this?)

Eric Martz, Karsten Theis

Personal tools