Sandbox Reserved 1672

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Revision as of 19:08, 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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Alginate Lyase, AlyC3

This protein has 2 large beta-sheets and 4 alpha-helices. The , binds with beta-sheet A. Beta-sheet A also contains most of the catalytic amino acids.

1 Function of your protein
2 Biological relevance and broader implications
3 Important amino acids
4 Structural highlights
5 Other important features

Function of your protein

Alginate lyase, AlyC3, comes from the Psychromonas organism. It is found mainly in algae.

The function of AlyC3 is to degrade alginate. AlyC3 plays a role in b-elimination at the glycosidic 1,4-O link. This generates oligosaccharides or monosaccharides.

insert rotating image of AlyC3 as a cartoon*

The known substrate for AlyC3 is polymannuronate (PM) and tetramannuronate.

Biological relevance and broader implications

Alginate is primarily found in algae and is the primary marine polysaccharides and carriers of the marine carbon cycle. Alginate lyase is synthesized by marine algae, mollusks, fungi, bacteria, and viruses.

Alginate lyase plays an important role in the treatment of lung infections, primarily in those with Cystic Fibrosis.

Alginate lyase is also important in environmental research dealing with biofuels and the recycling of alginate in the oceans.

Important amino acids

The ligands present in AlyC3 are the same as the substrate, polymannuronate and tetramannuronate, both sugars.

The catalytic amino acids in the binding site are His127 and Tyr 244. (Figure E) These residues act as the catalytic acid and base for the reaction. Tetramannuronate is cleaved in the active site and produces trisaccharides and monosaccharides.

Arg78 and Gln125 are also present and work to neutralize the negative charge on the carboxylic group.

Figure 5D shows the active site. show the catalytic triad amino acids and hydrogen bond with beta-sheets

Structural highlights

Secondary structures are alpha-helices and beta-sheets. The alpha helices are identified with the red color and the beta-sheets are identified with the blue color. There are two beta-sheets with 9 beta-strands in one and 7 beta-strands in the other. These sheets create what is called a jelly-roll fold with antiparallel strands and a hydrophobic interface. The secondary structures provide shape for the protein by creating a cleft and positively charged groove.

Tertiary (hydrogen bonds and disulfide bridge) and Quaternary(dimer) structure

space filling view- cleft

Other important features

Alginate Lyase has a channel where the sugar sits in. This channel is positively charged for the negatively charged sugar chain. The protein cleaves the sugar at the 0 site. The mutant of alginate lyase does not cleave the sugar right away.

Alginate Lyase contains a disulfide bond from Cys169-Cys183. This is used to stabilize the tertiary and quaternary structure of the protein.

== References == ^[1]

↑ 32967968

^[1]

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Sandbox Reserved 1672

From Proteopedia

Revision as of 19:08, 17 April 2021

Alginate Lyase, AlyC3

Contents

Function of your protein

Biological relevance and broader implications

Important amino acids

Structural highlights

Other important features

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@@ Line 37: / Line 37: @@
 Secondary structures are alpha-helices and beta-sheets. The alpha helices are identified with the red color and the beta-sheets are identified with the blue color. There are two beta-sheets with 9 beta-strands in one and 7 beta-strands in the other. These sheets create what is called a jelly-roll fold with antiparallel strands and a hydrophobic interface. The secondary structures provide shape for the protein by creating a cleft and positively charged groove.
-Tertiary and Quaternary structure
+Tertiary (hydrogen bonds and disulfide bridge) and Quaternary(dimer) structure
+space filling view- cleft
 == Other important features ==
-This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
+Alginate Lyase has a channel where the sugar sits in. This channel is positively charged for the negatively charged sugar chain. The protein cleaves the sugar at the 0 site. The mutant of alginate lyase does not cleave the sugar right away.
+Alginate Lyase contains a disulfide bond from Cys169-Cys183. This is used to stabilize the tertiary and quaternary structure of the protein.
 </StructureSection>