1d6y: Difference between revisions

Revision as of 13:13, 21 February 2008

CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE.

OverviewOverview

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.

About this StructureAbout this Structure

1D6Y is a Single protein structure of sequence from Escherichia coli with , , , , and as ligands. Active as Amine oxidase (copper-containing), with EC number 1.4.3.6 Full crystallographic information is available from OCA.

ReferenceReference

Visualization of dioxygen bound to copper during enzyme catalysis., Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE, Science. 1999 Nov 26;286(5445):1724-8. PMID:10576737

Page seeded by OCA on Thu Feb 21 12:13:40 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1d6y.jpg|left|200px]]<br /><applet load="1d6y" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1d6y.jpg|left|200px]]<br /><applet load="1d6y" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1d6y, resolution 2.4&Aring;" />
 '''CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE.'''<br />
 ==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.
+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.
 ==About this Structure==
-D6Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CU, CA, HY1, NO, PEA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D6Y OCA].
+D6Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HY1:'>HY1</scene>, <scene name='pdbligand=NO:'>NO</scene>, <scene name='pdbligand=PEA:'>PEA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D6Y OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Hajdu, J.]]
-[[Category: Knowles, P.F.]]
+[[Category: Knowles, P F.]]
-[[Category: McPherson, M.J.]]
+[[Category: McPherson, M J.]]
-[[Category: Phillips, S.E.V.]]
+[[Category: Phillips, S E.V.]]
-[[Category: Wilmot, C.M.]]
+[[Category: Wilmot, C M.]]
 [[Category: CA]]
 [[Category: CU]]
@@ Line 27: / Line 27: @@
 [[Category: reaction intermediate mimic]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:03:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:40 2008''