Lipase lid morph: Difference between revisions

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<Structure load='1lpm' size='400' frame='true' align='right' caption='Candida rugosa lipase ([[1trh]], [[1lpm]]).' scene='' />
<Structure load='' size='400' frame='true' align='right' caption='Candida rugosa lipase ([[1trh]], [[1lpm]]).' scene='Lipase_lid_morph/Lightseagreen_hinge/1' />
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]].
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" closed ([[1trh]]) or open ([[1lpm]])<ref name='2states1994'>PMID: 8142901</ref>. A morph<ref>This is a [[Morphs#Linear_Interpolation|linear interpolation morph]]. The 14-model PDB file is [[Image:Morph-linear-1trh-1lpm.pdb.gz]].</ref> shows the lid opening and closing.
''Candida rugosa'' lipase (triacylglycerol hydrolase) has been observed in two conformations, with the "lid" (residues 66-92<ref name='2states1994' />) closed ([[1trh]]) or open ([[1lpm]])<ref name='2states1994'>PMID: 8142901</ref>.


<scene name='Lipase_lid_morph/Rainbow/1'>TextToBeDisplayed</scene>
*Closed <font color='lightseagreen'><b>LID</b></font> (<scene name='Lipase_lid_morph/Lightseagreen_hinge/1'>restore initial scene</scene>).
*<scene name='Lipase_lid_morph/Lightseagreen_hinge/4'>Open</scene> <font color='lightseagreen'><b>LID</b></font> with inhibitor (1R)-menthyl hexyl phosphonate (<b><font color='#909090'>C</font> <font color='#ff0d0d'>O</font> <font color='#ff8000'>P</font></b>).


When open, substrate can access the catalytic triad, Ser209, Glu341, and His449<ref name='2states1994' />
A morph<ref>This is a [[Morphs#Linear_Interpolation|linear interpolation morph]]. The 14-model PDB file is [[Image:Morph-linear-1trh-1lpm.pdb.gz]].</ref> shows the lid opening and closing.
*<scene name='Lipase_lid_morph/Lightseagreen_hinge/2'>Cartoon morph</scene> (<font color='lightseagreen'><b>LID</b></font>).
*<scene name='Lipase_lid_morph/Lightseagreen_hinge/3'>Spacefilling morph</scene> (<font color='lightseagreen'><b>LID</b></font>, <font color='orange'><b>catalytic triad: Ser209, Glu341, and His449</b></font><ref name='2states1994' />).<br>
{{Template:Button Toggle Animation2}}
 
When the lid is closed, the enzyme surface is largely {{Template:ColorKey_Polar}}. When the lid opens, a {{Template:ColorKey_Hydrophobic}} pocket is exposed with the catalytic triad in the bottom.
 
*<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==

Latest revision as of 13:18, 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 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 AlsoSee Also

Notes and ReferencesNotes 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 File:Morph-linear-1trh-1lpm.pdb.gz.
  3. This is a rigid body morph based on the superposition in PDB file File:1TRH 1LPM.pdb. It is created by the Storymorph script on the fly.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Eric Martz, Karsten Theis