2bt3

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[[Image:2bt3.gif|left|200px]]
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{{STRUCTURE_2bt3| PDB=2bt3 | SCENE= }}
{{STRUCTURE_2bt3| PDB=2bt3 | SCENE= }}
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'''AGAO IN COMPLEX WITH RUTHENIUM-C4-WIRE AT 1.73 ANGSTROMS'''
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===AGAO IN COMPLEX WITH RUTHENIUM-C4-WIRE AT 1.73 ANGSTROMS===
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==Overview==
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Molecular wires comprising a Ru(II)- or Re(I)-complex head group, an aromatic tail group, and an alkane linker reversibly inhibit the activity of the copper amine oxidase from Arthrobacter globiformis (AGAO), with K(i) values between 6 muM and 37 nM. In the crystal structure of a Ru(II)-wire:AGAO conjugate, the wire occupies the AGAO active-site substrate access channel, the trihydroxyphenylalanine quinone cofactor is ordered in the "off-Cu" position with its reactive carbonyl oriented toward the inhibitor, and the "gate" residue, Tyr-296, is in the "open" position. Head groups, tail-group substituents, and linker lengths all influence wire-binding interactions with the enzyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 16157884 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16157884}}
==About this Structure==
==About this Structure==
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[[Category: Ruthenium diimine wire]]
[[Category: Ruthenium diimine wire]]
[[Category: Tpq]]
[[Category: Tpq]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:45:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:47:17 2008''

Revision as of 10:47, 27 July 2008

Image:2bt3.png

Template:STRUCTURE 2bt3

AGAO IN COMPLEX WITH RUTHENIUM-C4-WIRE AT 1.73 ANGSTROMS

Template:ABSTRACT PUBMED 16157884

About this Structure

2BT3 is a Single protein structure of sequence from Arthrobacter globiformis. Full crystallographic information is available from OCA.

Reference

Reversible inhibition of copper amine oxidase activity by channel-blocking ruthenium(II) and rhenium(I) molecular wires., Contakes SM, Juda GA, Langley DB, Halpern-Manners NW, Duff AP, Dunn AR, Gray HB, Dooley DM, Guss JM, Freeman HC, Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13451-6. Epub 2005 Sep 12. PMID:16157884

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