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Sandbox Reserved 1496

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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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This protein consists of 2 sequence-identical polypeptide chains of 287 amino acids.
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This enzyme is involved in step 1 of the subpathway that synthesizes staphyloxanthin from farnesyl diphosphate.
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It is present in Staphyloccocus aureus. It has 6 Magnesium ions, 2 Pyrophosphate 2-, 1 L(+)-tartaric acid and 2 (3r)-3-biphenyl-4-yl-1-azabicyclo[2.2.2]octan-3-ol as ligands (substrate or inhibitors, prosthetic groups, cofactors, carbohydrate, metal ions, regardless of whether these are covalently or non-covalently bound to the protein or nucleic acid chains).
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== Function ==
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This protein is involved in step 1 of the subpathway that synthesizes staphyloxanthin from farnesyl diphosphate.
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This subpathway is part of the pathway staphyloxanthin biosynthesis, which is itself part of Carotenoid biosynthesis.
This subpathway is part of the pathway staphyloxanthin biosynthesis, which is itself part of Carotenoid biosynthesis.
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== Molecular function ==
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Staphyloxanthin is a carotenoid, which is responsible for the golden color of S. aureus, and also play the role of virulence factor : it has an antioxidant action that helps the microbe evade death by reactive oxygen species produced by the host immune system.
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CrtM catalyses the first step of the synthesis of staphyloxanthin with a 2-step mechanism.
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== Function ==
Transferase Activity
Transferase Activity
Metal Ion Binding
Metal Ion Binding
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== Structure ==
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This protein consists of 2 sequence-identical polypeptide chains of 287 amino acids.
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It has 6 Magnesium ions, 2 Pyrophosphate 2-, 1 L(+)-tartaric acid and 2 (3r)-3-biphenyl-4-yl-1-azabicyclo[2.2.2]octan-3-ol as ligands (substrate or inhibitors, prosthetic groups, cofactors, carbohydrate, metal ions, regardless of whether these are covalently or non-covalently bound to the protein or nucleic acid chains).
== Biological process ==
== Biological process ==

Revision as of 14:03, 28 December 2018

This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.
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

Structure of Dehydrosqualene Synthase (Crtm)

Caption for this structure

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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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