View source for 2cfk


==AGAO in complex with wc5 (Ru-wire inhibitor, 5-carbon linker)==
<StructureSection load='2cfk' size='340' side='right'caption='[[2cfk]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2cfk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_globiformis"_(conn_1928)_bergey_et_al._1930 "achromobacter globiformis" (conn 1928) bergey et al. 1930]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CFK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=R5A:RUTHENIUM+WIRE,+5+CARBON+LINKER'>R5A</scene>, <scene name='pdbligand=R5B:RUTHENIUM+WIRE+WC5'>R5B</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1av4|1av4]], [[1avk|1avk]], [[1avl|1avl]], [[1iqx|1iqx]], [[1iqy|1iqy]], [[1iu7|1iu7]], [[1ivu|1ivu]], [[1ivv|1ivv]], [[1ivw|1ivw]], [[1ivx|1ivx]], [[1rjo|1rjo]], [[1sih|1sih]], [[1sii|1sii]], [[1ui7|1ui7]], [[1ui8|1ui8]], [[1w4n|1w4n]], [[1w5z|1w5z]], [[1w6c|1w6c]], [[1w6g|1w6g]], [[1wmn|1wmn]], [[1wmo|1wmo]], [[1wmp|1wmp]], [[2bt3|2bt3]], [[2cfd|2cfd]], [[2cfg|2cfg]], [[2cfl|2cfl]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.21 and 1.4.3.22 1.4.3.21 and 1.4.3.22] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfk OCA], [http://pdbe.org/2cfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cfk RCSB], [http://www.ebi.ac.uk/pdbsum/2cfk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cfk ProSAT]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cfk_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cfk ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The copper amine oxidase from Arthrobacter globiformis (AGAO) is reversibly inhibited by molecular wires comprising a Ru(II) complex head group and an aromatic tail group joined by an alkane linker. The crystal structures of a series of Ru(II)-wire-AGAO complexes differing with respect to the length of the alkane linker have been determined. All wires lie in the AGAO active-site channel, with their aromatic tail group in contact with the trihydroxyphenylalanine quinone (TPQ) cofactor of the enzyme. The TPQ cofactor is consistently in its active ("off-Cu") conformation, and the side chain of the so-called "gate" residue Tyr296 is consistently in the "gate-open" conformation. Among the wires tested, the most stable complex is produced when the wire has a -(CH2)4- linker. In this complex, the Ru(II)(phen)(bpy)2 head group is level with the protein molecular surface. Crystal structures of AGAO in complex with optically pure forms of the C4 wire show that the linker and head group in the two enantiomers occupy slightly different positions in the active-site channel. Both the Lambda and Delta isomers are effective competitive inhibitors of amine oxidation. Remarkably, inhibition by the C4 wire shows a high degree of selectivity for AGAO in comparison with other copper-containing amine oxidases.

Enantiomer-specific binding of ruthenium(II) molecular wires by the amine oxidase of Arthrobacter globiformis.,Langley DB, Brown DE, Cheruzel LE, Contakes SM, Duff AP, Hilmer KM, Dooley DM, Gray HB, Guss JM, Freeman HC J Am Chem Soc. 2008 Jun 25;130(25):8069-78. Epub 2008 May 29. PMID:18507382<ref>PMID:18507382</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2cfk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Copper Amine Oxidase|Copper Amine Oxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oxidoreductase]]
[[Category: Contakes, S M]]
[[Category: Dooley, D M]]
[[Category: Duff, A P]]
[[Category: Dunn, A R]]
[[Category: Freeman, H C]]
[[Category: Gray, H B]]
[[Category: Guss, J M]]
[[Category: Halpern-Manners, N W]]
[[Category: Juda, G A]]
[[Category: Langley, D B]]
[[Category: Amine oxidase]]
[[Category: Arthrobacter globiformi]]
[[Category: Competitive inhibition]]
[[Category: Copper]]
[[Category: Copper containing]]
[[Category: Cuao]]
[[Category: Metal-binding]]
[[Category: Quinone]]
[[Category: Ruthenium diimine wire]]
[[Category: Tpq]]