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1b8g
From Proteopedia
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| - | [[Image:1b8g.gif|left|200px]] | + | [[Image:1b8g.gif|left|200px]] |
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| - | '''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE''' | + | {{Structure |
| + | |PDB= 1b8g |SIZE=350|CAPTION= <scene name='initialview01'>1b8g</scene>, resolution 2.37Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B8G is a [ | + | 1B8G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Malus_x_domestica Malus x domestica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8G OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10610793 10610793] |
[[Category: 1-aminocyclopropane-1-carboxylate synthase]] | [[Category: 1-aminocyclopropane-1-carboxylate synthase]] | ||
[[Category: Malus x domestica]] | [[Category: Malus x domestica]] | ||
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[[Category: ethylene biosynthesis]] | [[Category: ethylene biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:07:39 2008'' |
Revision as of 08:07, 20 March 2008
| |||||||
| , resolution 2.37Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 10:07:39 2008
