This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
EPSP synthase
From Proteopedia
(Difference between revisions)
| Line 11: | Line 11: | ||
== Structural insights == | == Structural insights == | ||
| - | The enzyme has <scene name='57/570585/Two_domains/1'>two domains</scene>, with the active site found in the interdomain cleft. There is a substantial structural change upon substrate binding, resulting in a <scene name='57/570585/Closed_formation/1'>closed formation</scene>. Glyphosate (also known as Roundup) occupies the binding site of the second substrate, phosphoenol pyruvate. | + | The enzyme has <scene name='57/570585/Two_domains/1'>two domains</scene>, with the active site found in the interdomain cleft. There is a substantial structural change upon substrate binding, resulting in a <scene name='57/570585/Closed_formation/1'>closed formation</scene>. '''Glyphosate''' (also known as '''Roundup''') occupies the binding site of the second substrate, phosphoenol pyruvate. |
</StructureSection> | </StructureSection> | ||
Revision as of 21:26, 19 January 2016
Structure of EPSP Synthase
| |||||||||||
3D structures of EPSP synthase
Updated on 19-January-2016
References
- ↑ Priestman MA, Healy ML, Funke T, Becker A, Schonbrunn E. Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate. FEBS Lett. 2005 Oct 24;579(25):5773-80. PMID:16225867 doi:10.1016/j.febslet.2005.09.066
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Ann Taylor, Joel L. Sussman
