Lipase lid morph

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]).

Notes and ReferencesNotes 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 File:Morph-linear-1trh-1lpm.pdb.gz.

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Eric Martz, Karsten Theis

[2states1994-1] 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 File:Morph-linear-1trh-1lpm.pdb.gz.

[1]

[2]

Lipase lid morph

See AlsoSee Also

Notes and ReferencesNotes and References

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