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Lipase lid morph
From Proteopedia
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*<scene name='Lipase_lid_morph/Lightseagreen_hinge/5'>Spacefilling morph</scene> ({{Template:ColorKey_Polar}}, {{Template:ColorKey_Hydrophobic}}, <font color='orange'><b>catalytic triad: Ser209, Glu341, and His449</b></font><ref name='2states1994' />). | *<scene name='Lipase_lid_morph/Lightseagreen_hinge/5'>Spacefilling morph</scene> ({{Template:ColorKey_Polar}}, {{Template:ColorKey_Hydrophobic}}, <font color='orange'><b>catalytic triad: Ser209, Glu341, and His449</b></font><ref name='2states1994' />). | ||
| + | |||
| + | An alternate morph<ref>This is a rigid body morph based on the superposition in PDB file [[Image:1TRH_1LPM.pdb]]. It is created by the [[Jmol/Storymorph|Storymorph script]] on the fly.</ref> shows a different path between the <scene name='49/493694/Storymorph/1'>same initial and final experimental structures</scene>. 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. | ||
| + | |||
| + | <jmol> | ||
| + | <jmolButton> | ||
| + | <script>script "https://proteopedia.org/wiki/images/a/a2/Storymorph.spt"; | ||
| + | domain2 = {(75-85)}; | ||
| + | model 2; | ||
| + | structures = [{1.2}, {1.1}]; | ||
| + | domains = [ | ||
| + | [{protein and not domain2}], | ||
| + | [{domain2}, {(74,86) and *.CA}], | ||
| + | ]; | ||
| + | morph_palindrome = 1; | ||
| + | morph(15,structures,domains);</script> | ||
| + | <text>Run alternate morph</text> | ||
| + | </jmolButton> | ||
| + | </jmol> | ||
==See Also== | ==See Also== | ||
Current revision
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
- Lipase, the main article in Proteopedia.
- Molecular Playground/Pancreatic Lipase
- Lipase in Wikipedia
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.
- ↑ 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.
