2bt3: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:
[[Image:2bt3.png|left|200px]]
==AGAO IN COMPLEX WITH RUTHENIUM-C4-WIRE AT 1.73 ANGSTROMS==
<StructureSection load='2bt3' size='340' side='right' caption='[[2bt3]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bt3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BT3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BT3 FirstGlance]. <br>
</td></tr><tr><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=R4A:BIS[1H,1H-2,2-BIPYRIDINATO(2-)-KAPPA~2~N~1~,N~1~]{3-[4-(1,10-DIHYDRO-1,10-PHENANTHROLIN-4-YL-KAPPA~2~N~1~,N~10~)BUTOXY]-N,N-DIMETHYLANILINATO(2-)}RUTHENIUM'>R4A</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
<tr><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><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]]</td></tr>
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bt3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bt3 RCSB], [http://www.ebi.ac.uk/pdbsum/2bt3 PDBsum]</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/bt/2bt3_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_2bt3|  PDB=2bt3  |  SCENE=  }}
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<ref>PMID:16157884</ref>


===AGAO IN COMPLEX WITH RUTHENIUM-C4-WIRE AT 1.73 ANGSTROMS===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_16157884}}
 
==About this Structure==
[[2bt3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BT3 OCA].


==See Also==
==See Also==
*[[Copper Amine Oxidase|Copper Amine Oxidase]]
*[[Copper Amine Oxidase|Copper Amine Oxidase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:016157884</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Arthrobacter globiformis]]
[[Category: Arthrobacter globiformis]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]

Revision as of 06:13, 29 September 2014

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

Structural highlights

2bt3 is a 1 chain structure with sequence from Arthrobacter globiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
NonStd Res:
Related:1av4, 1avk, 1avl, 1iqx, 1iqy, 1iu7, 1ivu, 1ivv, 1ivw, 1ivx, 1rjo, 1sih, 1sii, 1ui7, 1ui8, 1w4n, 1w5z, 1w6c, 1w6g
Activity:Oxidoreductase, with EC number and 1.4.3.22 1.4.3.21 and 1.4.3.22
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

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

2bt3, resolution 1.73Å

Drag the structure with the mouse to rotate

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

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2bt3&oldid=1999639"