1d6z: Difference between revisions

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[[Image:1d6z.~~gif~~|left|200px]]

[[Image:1d6z.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER-CONTAINING AMINE OXIDASE.~~'''~~

===CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER-CONTAINING AMINE OXIDASE.===

~~==Overview==~~

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X-~~ray crystal structures of three species related to the oxidative half of the reaction of the copper~~-~~containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate~~, ~~and structures were determined~~ to ~~resolutions between 2.1 and 2.4 angstroms. The oxidation state of~~ the ~~quinone cofactor was investigated by single-crystal spectrophotometry~~. ~~The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction~~. ~~The quinone cofactor~~ is ~~regenerated from~~ the ~~iminoquinone intermediate by hydrolysis involving Asp383, the catalytic base in the reductive half~~-~~reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate~~-~~determining step of the reaction in the crystal.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10576737}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10576737 is the PubMed ID number.

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==About this Structure==

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[[Category: Wilmot, C M.]]

[[Category: Reaction intermediate]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:31:18 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:33:37 2008''

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-[[Image:1d6z.gif|left|200px]]
+{{Seed}}
+[[Image:1d6z.png|left|200px]]
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 {{STRUCTURE_1d6z|  PDB=1d6z  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER-CONTAINING AMINE OXIDASE.'''
+===CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER-CONTAINING AMINE OXIDASE.===
-==Overview==
+<!--
-X-ray crystal structures of three species related to the oxidative half of the reaction of the copper-containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate, and structures were determined to resolutions between 2.1 and 2.4 angstroms. The oxidation state of the quinone cofactor was investigated by single-crystal spectrophotometry. The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction. The quinone cofactor is regenerated from the iminoquinone intermediate by hydrolysis involving Asp383, the catalytic base in the reductive half-reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate-determining step of the reaction in the crystal.
+The line below this paragraph, {{ABSTRACT_PUBMED_10576737}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10576737 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10576737}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Wilmot, C M.]]
 [[Category: Reaction intermediate]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:31:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:33:37 2008''