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Little is known what the ybiL protein is supposed to do. From the NMR study in the context of the Protein Structure Initiative and NESG consortium, large portions of it are disordered with some (possibly transient) helices on both the N- and C-terminal arms. This was supported by the NMR chemical shifts. The central domain is a Zinc finger with a <scene name='80/807434/Zinc_coordination/1'>Tetrahedral coordination of the Zn2+ ion by 4 Cys residues</scene>.
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Little is known what the ybiL protein is supposed to do. From the NMR study in the context of the Protein Structure Initiative and NESG consortium, large portions of it are disordered with some (possibly transient) helices on both the N- and C-terminal arms. This was supported by the NMR chemical shifts. The central domain is a Zinc finger with a <scene name='80/807434/Zinc_coordination/1'>tetrahedral coordination of the Zn2+ ion by 4 Cys residues</scene>.
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.

Revision as of 14:08, 31 January 2019

Strasbourg course on creating Proteopedia pages - an uncharacterised protein ybiL from E. Coli

Zinc coordination residues

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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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