Sandbox Reserved 1673

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{{Sandbox_Reserved_BHall_Sp21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
{{Sandbox_Reserved_BHall_Sp21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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==Your Heading Here (maybe something like 'Structure')==
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==Structure of AlyC3==
<StructureSection load='7c8g' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='7c8g' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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== Function of your protein ==
== Function of your protein ==
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AlyC3 is an <scene name='87/873235/Protein_view_2/1'>enzyme</scene> present in Psychromonas sp. C-3 that plays a role in β-elimination at the glycosidic 1,4-O-linkage in alginate.
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AlyC3 is an <scene name='87/873235/Protein_view_2/1'>enzyme</scene> present in Psychromonas sp. C-3 that plays a role in β-elimination at the glycosidic 1,4-O-linkage in alginate. AlyC3 uses tetramannuronate or polymannuronate as its substrate and converts the polymer into its substituent monomers, shorter PM chains, and 4-deoxy-L-erythro-hex-4-enopyranosyluronic acid. This facilitates alginate degradation and recycling in marine ecosystems.
== Biological relevance and broader implications ==
== Biological relevance and broader implications ==
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The protein PL7 alginate lyase AlyC3 plays roles in the degradation of alginate in the ocean
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The protein PL7 alginate lyase AlyC3 plays roles in the degradation of alginate in the ocean. Alginate lyases are made by bacteria, viruses, fungi, marine algae, and marine molusks. Alginate lyases have a variety of potential applications in the food, agriculture, and pharmaceutical industries. They may even be used to treat chronic lung infections by ''Pseudomonas aeruginosa.'' Exolytic and endolytic alginate lyases working in conjunction also have the potential to produce biofuels by breaking down alginate-rich algal cell walls into monosaccharides.
== Important amino acids==
== Important amino acids==
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he residues His127, and Tyr244 are important for the catalytic function of AlyC3 as
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The residues His127, and Tyr244 are important for the catalytic function of AlyC3 as
mutating either or both amino acids to an alanine resulted in an almost inactive enzyme.
mutating either or both amino acids to an alanine resulted in an almost inactive enzyme.
It is believed that Arg82 and Tyr190 at the two ends of the catalytic canyon are the most important residues for binding and
It is believed that Arg82 and Tyr190 at the two ends of the catalytic canyon are the most important residues for binding and
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== Structural highlights ==
== Structural highlights ==
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Alginate lyase has two domains with Cyclic – C2 symmetry. Its secondary structure is
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AlyC3 has two domains with Cyclic – C2 symmetry. Its secondary structure is
approximately 14% helices and 44% beta strands. Both domains each consist of 7 helices and 15 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.
approximately 14% helices and 44% beta strands. Both domains each consist of 7 helices and 15 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.

Revision as of 22:58, 17 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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More help: Help:Editing

Structure of AlyC3

Caption for this structure

Drag the structure with the mouse to rotate

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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