Sandbox Reserved 1072: Difference between revisions
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{{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==Diguanylate Cyclase DgcZ from Escherichia coli== | ==Diguanylate Cyclase DgcZ from Escherichia coli== | ||
<StructureSection load=' | <StructureSection load='4H54' size='340' side='right' caption='Diguanylate Cyclase DgcZ' scene=''> | ||
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
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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====3His/1Cys Motif==== | ====3His/1Cys Motif==== | ||
== Mechanism of Action == | == Mechanism of Action == | ||
<scene name='69/694239/Hydrophobicity_int_residues/1'>Hydrophobic regions</scene> on the alpha helices of the zinc binding domain participate in van der waals interactions that induce a conformational change in the protein when zinc binds. | <scene name='69/694239/Hydrophobicity_int_residues/1'>Hydrophobic regions</scene> on the alpha helices of the zinc binding domain participate in van der waals interactions that induce a conformational change in the protein when zinc binds. When Zinc binds, the <scene name='69/694239/Czbd_with_helices_labeled/2'>𝝰1 helix</scene> becomes straightened, burying nonpolar side-chain residues, influencing activity of DgcZ | ||
== Zinc Ligand(s) == | == Zinc Ligand(s) == | ||
The two <scene name='69/694239/Zinc_binding_domain/1'>Zinc binding domains</scene> of Diguanylate Cyclase binds a single zinc ion each, for a total of two zinc ions. | The two <scene name='69/694239/Zinc_binding_domain/1'>Zinc binding domains</scene> of Diguanylate Cyclase binds a single zinc ion each, for a total of two zinc ions. | ||
Revision as of 20:44, 24 March 2017
| This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080. |
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Diguanylate Cyclase DgcZ from Escherichia coliDiguanylate Cyclase DgcZ from Escherichia coli
This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. Biological Function Structural OverviewGGDEF DomainZinc Binding Domain3His/1Cys MotifMechanism of Actionon the alpha helices of the zinc binding domain participate in van der waals interactions that induce a conformational change in the protein when zinc binds. When Zinc binds, the becomes straightened, burying nonpolar side-chain residues, influencing activity of DgcZ Zinc Ligand(s)The two of Diguanylate Cyclase binds a single zinc ion each, for a total of two zinc ions. Other LigandsThis is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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ReferencesReferences
- ↑ 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
- ↑ 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