1w9y
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1w9y.gif|left|200px]] | + | [[Image:1w9y.gif|left|200px]] |
| - | + | ||
| - | '''THE STRUCTURE OF ACC OXIDASE''' | + | {{Structure |
| + | |PDB= 1w9y |SIZE=350|CAPTION= <scene name='initialview01'>1w9y</scene>, resolution 2.1Å | ||
| + | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Aminocyclopropanecarboxylate_oxidase Aminocyclopropanecarboxylate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.4 1.14.17.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE STRUCTURE OF ACC OXIDASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1W9Y is a [ | + | 1W9Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Petunia_x_hybrida Petunia x hybrida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W9Y OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme., Zhang Z, Ren JS, Clifton IJ, Schofield CJ, Chem Biol. 2004 Oct;11(10):1383-94. PMID:[http:// | + | Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme., Zhang Z, Ren JS, Clifton IJ, Schofield CJ, Chem Biol. 2004 Oct;11(10):1383-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15489165 15489165] |
[[Category: Aminocyclopropanecarboxylate oxidase]] | [[Category: Aminocyclopropanecarboxylate oxidase]] | ||
[[Category: Petunia x hybrida]] | [[Category: Petunia x hybrida]] | ||
| Line 23: | Line 32: | ||
[[Category: acco]] | [[Category: acco]] | ||
| - | ''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 14:54:15 2008'' |
Revision as of 12:54, 20 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Aminocyclopropanecarboxylate oxidase, with EC number 1.14.17.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF ACC OXIDASE
Overview
The final step in the biosynthesis of the plant signaling molecule ethylene is catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase (ACCO). ACCO requires bicarbonate as an activator and catalyzes the oxidation of ACC to give ethylene, CO2, and HCN. We report crystal structures of ACCO in apo-form (2.1 A resolution) and complexed with Fe(II) (2.55 A) or Co(II) (2.4 A). The active site contains a single Fe(II) ligated by three residues (His177, Asp179, and His234), and it is relatively open compared to those of the 2-oxoglutarate oxygenases. The side chains of Arg175 and Arg244, proposed to be involved in binding bicarbonate, project away from the active site, but conformational changes may allow either or both to enter the active site. The structures will form a basis for future mechanistic and inhibition studies.
About this Structure
1W9Y is a Single protein structure of sequence from Petunia x hybrida. Full crystallographic information is available from OCA.
Reference
Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme., Zhang Z, Ren JS, Clifton IJ, Schofield CJ, Chem Biol. 2004 Oct;11(10):1383-94. PMID:15489165
Page seeded by OCA on Thu Mar 20 14:54:15 2008
