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== Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. ==
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<Structure load='Insert PDB code or filename here' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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==Title==
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<Structure load='1pgb' size='300' frame='true' align='right' caption=' Torpedo acetylcholinesterase' scene='Insert optional scene name here' />
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===subtitle===
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PubMed Abstract:
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<ref>PMID:3023912</ref>
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Binding sites of Torpedo acetylcholinesterase (EC 3.1.1.7) for quaternary ligands were investigated by x-ray crystallography and photoaffinity labeling. Crystal structures of complexes with ligands were determined at 2.8-A resolution. In a complex with edrophonium, and quaternary nitrogen of the ligand interacts with the indole of Trp-84, and its m-hydroxyl displays bifurcated hydrogen bonding to two members of the catalytic triad, Ser-200 and His-440. In a complex with tacrine, the acridine is stacked against the indole of Trp-84. The bisquaternary ligand decamethonium is oriented along the narrow gorge leading to the active site; one quaternary group is apposed to the indole of Trp-84 and the other to that of Trp-279, near the top of the gorge. The only major conformational difference between the three complexes is in the orientation of the phenyl ring of Phe-330. In the decamethonium complex it lies parallel to the surface of the gorge; in the other two complexes it is positioned to make contact with the bound ligand. This close interaction was confirmed by photoaffinity labelling by the photosensitive probe 3H-labeled p-(N,N-dimethylamino)benzenediazonium fluoroborate, which labeled, predominantly, Phe-330 within the active site. Labeling of Trp-279 was also observed. One mole of label is incorporated per mole of AcChoEase inactivated, indicating that labeling of Trp-279 and that of Phe-330 are mutually exclusive. The structural and chemical data, together, show the important role of aromatic groups as binding sites for quaternary ligands, and they provide complementary evidence assigning Trp-84 and Phe-330 to the "anionic" subsite of the active site and Trp-279 to the "peripheral" anionic site.
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<ref>PMID:7120407</ref>
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<ref>PMID: 2337600</ref>
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<ref>PMID:7308213</ref>
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<ref>PMID:17615299</ref>
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[[Image:MW_Folding_Simulations.gif]]
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<Structure load='' size='400' frame='true' align='right' caption='Candida rugosa lipase ([[1trh]], [[1lpm]]).' scene='Lipase_lid_morph/Lightseagreen_hinge/1' />
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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]].
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''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>.
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<scene name='Sandbox_UC_9/Arcoiris2/2'>hermoso y desconocido </scene>
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*Closed <font color='lightseagreen'><b>LID</b></font> (<scene name='Lipase_lid_morph/Lightseagreen_hinge/1'>restore initial scene</scene>).
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*<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>).
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lalalala
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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.
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*<scene name='Lipase_lid_morph/Lightseagreen_hinge/2'>Cartoon morph</scene> (<font color='lightseagreen'><b>LID</b></font>).
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*<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>
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{{Template:Button Toggle Animation2}}
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{{Template:ColorKey_Amino2CarboxyRainbow}}
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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.
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<quiz display=simple>
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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' />).
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{que dia es hoy?...
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|type="()"}
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- lunes
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+ miercoles
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- sabado
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</quiz>
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==See Also==
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*[[Lipase]], the main article in Proteopedia.
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*[[Molecular Playground/Pancreatic Lipase]]
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*[http://en.wikipedia.org/wiki/Lipase Lipase in Wikipedia]
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<Structure load='1acj' size='300' frame='true' align='center' caption='Insert caption here' scene='Insert optional scene name here' />
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==Notes and References==
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<references />
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<scene name='Sandbox_UC_9/Tacrine/2'>escena nueva</scene>
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Current revision

Insert caption here

Drag the structure with the mouse to rotate

Contents

Title

subtitle

[1]  
[2]  
[3]  
[4]   
[5]

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[6]) closed (1trh) or open (1lpm)[6].

  • Closed LID ().
  • LID with inhibitor (1R)-menthyl hexyl phosphonate (C O P).

A morph[7] shows the lid opening and closing.

  • (LID).
  • (LID, catalytic triad: Ser209, Glu341, and His449[6]).


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[6]).

See Also

Notes and References

  1. ↑ Kim KS, Rosenkrantz MS, Guarente L. Saccharomyces cerevisiae contains two functional citrate synthase genes. Mol Cell Biol. 1986 Jun;6(6):1936-42. PMID:3023912
  2. ↑ Remington S, Wiegand G, Huber R. Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution. J Mol Biol. 1982 Jun 15;158(1):111-52. PMID:7120407
  3. ↑ Karpusas M, Branchaud B, Remington SJ. Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A. Biochemistry. 1990 Mar 6;29(9):2213-9. PMID:2337600
  4. ↑ Bayer E, Bauer B, Eggerer H. Evidence from inhibitor studies for conformational changes of citrate synthase. Eur J Biochem. 1981 Nov;120(1):155-60. PMID:7308213
  5. ↑ Lee YJ, Hoe KL, Maeng PJ. Yeast cells lacking the CIT1-encoded mitochondrial citrate synthase are hypersusceptible to heat- or aging-induced apoptosis. Mol Biol Cell. 2007 Sep;18(9):3556-67. Epub 2007 Jul 5. PMID:17615299 doi:10.1091/mbc.E07-02-0118
  6. ↑ 6.0 6.1 6.2 6.3 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
  7. ↑ This is a linear interpolation morph. The 14-model PDB file is Image:Morph-linear-1trh-1lpm.pdb.gz.
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