1d6z
From Proteopedia
(New page: 200px<br /><applet load="1d6z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d6z, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1d6z.gif|left|200px]]<br /><applet load="1d6z" size=" | + | [[Image:1d6z.gif|left|200px]]<br /><applet load="1d6z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1d6z, resolution 2.1Å" /> | caption="1d6z, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER-CONTAINING AMINE OXIDASE.'''<br /> | '''CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER-CONTAINING AMINE OXIDASE.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | X-ray crystal structures of three species related to the oxidative half of | + | 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== | ==About this Structure== | ||
| - | 1D6Z 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, PEO, 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:// | + | 1D6Z 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=PEO:'>PEO</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=1D6Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hajdu, J.]] | [[Category: Hajdu, J.]] | ||
| - | [[Category: Knowles, P | + | [[Category: Knowles, P F.]] |
| - | [[Category: McPherson, M | + | [[Category: McPherson, M J.]] |
| - | [[Category: Phillips, S | + | [[Category: Phillips, S E.V.]] |
| - | [[Category: Wilmot, C | + | [[Category: Wilmot, C M.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: reaction intermediate]] | [[Category: reaction intermediate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:38 2008'' |
Revision as of 10:13, 21 February 2008
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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.
About this Structure
1D6Z 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.
Reference
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 12:13:38 2008
Categories: Amine oxidase (copper-containing) | Escherichia coli | Single protein | Hajdu, J. | Knowles, P F. | McPherson, M J. | Phillips, S E.V. | Wilmot, C M. | CA | CU | GOL | HY1 | PEA | PEO | Reaction intermediate
