1wa6
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1wa6 |SIZE=350|CAPTION= <scene name='initialview01'>1wa6</scene>, resolution 2.55Å | |PDB= 1wa6 |SIZE=350|CAPTION= <scene name='initialview01'>1wa6</scene>, resolution 2.55Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+X'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+X'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wa6 OCA], [http://www.ebi.ac.uk/pdbsum/1wa6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wa6 RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Schofield, C J.]] | [[Category: Schofield, C J.]] | ||
[[Category: Zhang, Z.]] | [[Category: Zhang, Z.]] | ||
| - | [[Category: FE2]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: SO4]] | ||
[[Category: 2og oxygenase]] | [[Category: 2og oxygenase]] | ||
[[Category: acc oxidase]] | [[Category: acc oxidase]] | ||
[[Category: acco]] | [[Category: acco]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:33:26 2008'' |
Revision as of 21:33, 30 March 2008
| |||||||
| , resolution 2.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Aminocyclopropanecarboxylate oxidase, with EC number 1.14.17.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
1WA6 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 Mon Mar 31 00:33:26 2008
