Lipase lid morph: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Eric Martz (talk | contribs)
No edit summary
Eric Martz (talk | contribs)
No edit summary
Line 10: Line 10:
*<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/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' />).
*<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' />).
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' />).


==See Also==
==See Also==

Revision as of 14:41, 14 May 2012

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]).

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.

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

Eric Martz, Karsten Theis