Sandbox Reserved 991

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== Structure ==
== Structure ==
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These are the <scene name='69/691533/Important_residues/1'>Important Residues</scene> for this protein. The first step is to open the epoxide ring on 2,3-oxidosqualene by protonation. The proton donor is the aspartic acid residue D455. Conversely, in the second step of the reaction, a proton is removed from C9 and is accepted by the histidine residue H232.
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These are the <scene name='69/691533/Important_residues/1'>Important Residues</scene> for this protein. The opening of the epoxide ring of 2,3-oxidosqualene requires protonation by the enzyme. The proton donor is the aspartic acid residue D455. Conversely, in the second step of the reaction, a proton is removed from C9 and is accepted by the histidine residue H232.
== Function ==
== Function ==

Revision as of 00:18, 24 February 2015

This Sandbox is Reserved from 20/01/2015, through 30/04/2016 for use in the course "CHM 463" taught by Mary Karpen at the Grand Valley State University. This reservation includes Sandbox Reserved 987 through Sandbox Reserved 996.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

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This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

Contents

Introduction

Lanosterol synthase is an important enzyme in the cholesterol biosynthesis pathway, it converts 2,3-Oxidosqualene to Lanosterol.

Image:Lanosterol synthase.jpg

Structure

These are the for this protein. The opening of the epoxide ring of 2,3-oxidosqualene requires protonation by the enzyme. The proton donor is the aspartic acid residue D455. Conversely, in the second step of the reaction, a proton is removed from C9 and is accepted by the histidine residue H232.

Function

The enzyme oxidosqualene cyclase carries out the most complex phase of cholesterol synthesis. It takes a lengthy skinny carbon chain, oxidosqualene, and folds it to create a cyclic compound composed of four connected rings.

Cholesterol Biosynthesis

Cholesterol

Disease

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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