1wa6

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{{STRUCTURE_1wa6| PDB=1wa6 | SCENE= }}
{{STRUCTURE_1wa6| PDB=1wa6 | SCENE= }}
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'''THE STRUCTURE OF ACC OXIDASE'''
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===THE STRUCTURE OF ACC OXIDASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15489165 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15489165}}
==About this Structure==
==About this Structure==
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[[Category: Acc oxidase]]
[[Category: Acc oxidase]]
[[Category: Acco]]
[[Category: Acco]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:22:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:53:45 2008''

Revision as of 15:53, 27 July 2008

Template:STRUCTURE 1wa6

THE STRUCTURE OF ACC OXIDASE

Template:ABSTRACT PUBMED 15489165

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

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