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-...) |
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| - | [[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== | ||
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[[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
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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
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