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Lipase lid morph

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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' />).
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A second morph<ref>This is a [[Jmol/Storymorph|rigid body morph]] based on the superoposition in PDB file is [[Image:1TRH_1LPM.pdb]].</ref> shows a <scene name='49/493694/Storymorph/1'>different path</scene> between the same initial and final experimental structures.
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An alternate morph<ref>This is a [[Jmol/Storymorph|rigid body morph]] based on the superoposition in PDB file is [[Image:1TRH_1LPM.pdb]].</ref> shows a <scene name='49/493694/Storymorph/1'>different path</scene> between the same initial and final experimental structures. 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.
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<jmol>
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<jmolButton>
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<script>script "https://proteopedia.org/wiki/images/a/a2/Storymorph.spt";
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domain2 = {(75-85)};
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model 2;
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structures = [{1.2}, {1.1}];
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domains = [
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[{protein and not domain2}],
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[{domain2}, {(74,86) and *.CA}],
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];
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morph_palindrome = 1;
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morph(15,structures,domains);</script>
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<text>Run alternate morph</text>
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</jmolButton>
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</jmol>
==See Also==
==See Also==

Revision as of 10:06, 10 August 2021

Candida rugosa lipase (1trh, 1lpm).

Drag the structure with the mouse to rotate

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 between the same initial and final experimental structures. 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 superoposition in PDB file is Image:1TRH 1LPM.pdb.

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Eric Martz, Karsten Theis

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