Sandbox Reserved 1673

From Proteopedia

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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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== Function ==
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== Function of your protein ==
AlyC3 is an <scene name='87/873235/Protein_view_2/1'>enzyme</scene> that is plays a role in β-elimination at the glycosidic 1,4-O-linkage in alginate.
AlyC3 is an <scene name='87/873235/Protein_view_2/1'>enzyme</scene> that is plays a role in β-elimination at the glycosidic 1,4-O-linkage in alginate.
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== Disease ==
 
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== Relevance ==
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== Biological relevance and broader implications ==
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== Structural highlights ==
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== Important amino acids==
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Alginate lyase has two domains with Cyclic – C2 symmetry. Its secondary structure is roughly 14% helices and 44% beta strands. Both domains each consist of 7 helices and 15 beta strands with one disulfide bridge. The most <scene name='87/873235/Important_residues_view/1'>important residues</scene> for binding substrate as well as those involved in catalysis all lie on beta strands in both domains.
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== Structural highlights ==
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strands with one disulfide bridge. The most <scene name='87/873235/Important_residues_view/1'>important residues</scene> for binding substrate as well as those involved in catalysis all lie on beta strands in both domains.
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== Other important features ==

Revision as of 13:56, 7 April 2021

This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682.
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References

[3]

  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
  3. Xu F, Chen XL, Sun XH, Dong F, Li CY, Li PY, Ding H, Chen Y, Zhang YZ, Wang P. Structural and molecular basis for the substrate positioning mechanism of a new PL7 subfamily alginate lyase from the Arctic. J Biol Chem. 2020 Sep 23. pii: RA120.015106. doi: 10.1074/jbc.RA120.015106. PMID:32967968 doi:http://dx.doi.org/10.1074/jbc.RA120.015106
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