Sandbox Reserved 1672
From Proteopedia
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==Alginate Lyase, AlyC3== | ==Alginate Lyase, 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 protein | + | Alginate lyase lives in a salty environment with an optimal pH of 8 and temperature of 22C. This protein consists of 2 large beta-sheets and 4 alpha-helices. Beta-sheet A contains most of the catalytic amino acids. There is a mutant of the is protein with the PDB ID 7C8F. The mutant contains dimannuronate. |
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Secondary structures are <scene name='87/873234/Secondary_structure/3'>alpha-helices and beta-sheets</scene>. 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. | Secondary structures are <scene name='87/873234/Secondary_structure/3'>alpha-helices and beta-sheets</scene>. 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. | ||
| - | The <scene name='87/873234/Tert_and_quat_structure/1'>tertiary structure in AlyC3</scene> is hydrogen bonds and a disulfide bridge. The hydrogen bonds help hold the helices together and are important in protein folding. The disulfide bridge is used to help stabilize the | + | The <scene name='87/873234/Tert_and_quat_structure/1'>tertiary structure in AlyC3</scene> is hydrogen bonds and a disulfide bridge. The hydrogen bonds help hold the helices together and are important in protein folding. The disulfide bridge is used to help stabilize the protein. The quaternary structure in AlyC3 is the dimer structure. A dimer is consisted of two monomers and helps increase the stability and availability of the active site. |
The <scene name='87/873234/Space_filling/1'>space-filling</scene> view shows the cleft in the protein. This cleft is where the active site is located and allows the substrate to attach. | The <scene name='87/873234/Space_filling/1'>space-filling</scene> view shows the cleft in the protein. This cleft is where the active site is located and allows the substrate to attach. | ||
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</StructureSection> | </StructureSection> | ||
| - | == References == <ref> 32967968 </ref> | + | == References == <ref> PMID 32967968 </ref> |
<references/> | <references/> | ||
| - | <ref> 32967968 </ref> | ||
Current revision
| 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
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== References == [1]
- ↑ 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
