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.
1b8g
From Proteopedia
(New page: 200px<br /><applet load="1b8g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b8g, resolution 2.37Å" /> '''1-AMINOCYCLOPROPANE-...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1b8g.gif|left|200px]]<br /><applet load="1b8g" size=" | + | [[Image:1b8g.gif|left|200px]]<br /><applet load="1b8g" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b8g, resolution 2.37Å" /> | caption="1b8g, resolution 2.37Å" /> | ||
'''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE'''<br /> | '''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 2.4 A crystal structure of the vitamin B6-dependent enzyme | + | The 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, and a completely different catalytic activity yet the overall folds and the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (external aldimine with ACC, i.e. with the product) has been modeled. The new structure provides a basis for the rational design of inhibitors with broad agricultural applications. |
==About this Structure== | ==About this Structure== | ||
| - | 1B8G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Malus_x_domestica Malus x domestica] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14] Full crystallographic information is available from [http:// | + | 1B8G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Malus_x_domestica Malus x domestica] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8G OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: Feng, L.]] | [[Category: Feng, L.]] | ||
[[Category: Hohenester, E.]] | [[Category: Hohenester, E.]] | ||
| - | [[Category: Jansonius, J | + | [[Category: Jansonius, J N.]] |
| - | [[Category: Kirsch, J | + | [[Category: Kirsch, J F.]] |
[[Category: Storici, P.]] | [[Category: Storici, P.]] | ||
[[Category: PLP]] | [[Category: PLP]] | ||
[[Category: ethylene biosynthesis]] | [[Category: ethylene biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:36 2008'' |
Revision as of 09:52, 21 February 2008
|
1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE
Overview
The 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, and a completely different catalytic activity yet the overall folds and the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (external aldimine with ACC, i.e. with the product) has been modeled. The new structure provides a basis for the rational design of inhibitors with broad agricultural applications.
About this Structure
1B8G is a Single protein structure of sequence from Malus x domestica with as ligand. Active as 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14 Full crystallographic information is available from OCA.
Reference
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene., Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN, J Mol Biol. 1999 Dec 3;294(3):745-56. PMID:10610793
Page seeded by OCA on Thu Feb 21 11:52:36 2008
