1n68: Difference between revisions

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{{Seed}}
[[Image:1n68.png|left|200px]]


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==Copper bound to the Multicopper Oxidase CueO==
The line below this paragraph, containing "STRUCTURE_1n68", creates the "Structure Box" on the page.
<StructureSection load='1n68' size='340' side='right'caption='[[1n68]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1n68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N68 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2C:CU-CL-CU+LINKAGE'>C2C</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
{{STRUCTURE_1n68|  PDB=1n68  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n68 OCA], [https://pdbe.org/1n68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n68 RCSB], [https://www.ebi.ac.uk/pdbsum/1n68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n68 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CUEO_ECOLI CUEO_ECOLI]
== 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/n6/1n68_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1n68 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CueO, a multicopper oxidase, is part of the copper-regulatory cue operon in Escherichia coli, is expressed under conditions of copper stress and shows enhanced oxidase activity when additional copper is present. The 1.7-A resolution structure of a crystal soaked in CuCl2 reveals a Cu(II) ion bound to the protein 7.5 A from the T1 copper site in a region rich in methionine residues. The trigonal bipyramidal coordination sphere is unusual, containing two methionine sulfur atoms, two aspartate carboxylate oxygen atoms, and a water molecule. Asp-439 both ligates the labile copper and hydrogen-bonds to His-443, which ligates the T1 copper. This arrangement may mediate electron transfer from substrates to the T1 copper. Mutation of residues bound to the labile copper results in loss of oxidase activity and of copper tolerance, confirming a regulatory role for this site. The methionine-rich portion of the protein, which is similar to that of other proteins involved in copper homeostasis, does not display additional copper binding. The type 3 copper atoms of the trinuclear cluster in the structure are bridged by a chloride ion that completes a square planar coordination sphere for the T2 copper atom but does not affect oxidase activity.


===Copper bound to the Multicopper Oxidase CueO===
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO.,Roberts SA, Wildner GF, Grass G, Weichsel A, Ambrus A, Rensing C, Montfort WR J Biol Chem. 2003 Aug 22;278(34):31958-63. Epub 2003 Jun 6. PMID:12794077<ref>PMID:12794077</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1n68" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12794077}}, adds the Publication Abstract to the page
*[[Blue copper oxidase CueO 3D structures|Blue copper oxidase CueO 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12794077 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12794077}}
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</StructureSection>
==About this Structure==
1N68 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N68 OCA].
 
==Reference==
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO., Roberts SA, Wildner GF, Grass G, Weichsel A, Ambrus A, Rensing C, Montfort WR, J Biol Chem. 2003 Aug 22;278(34):31958-63. Epub 2003 Jun 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12794077 12794077]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ambrus, A.]]
[[Category: Ambrus A]]
[[Category: Grass, G.]]
[[Category: Grass G]]
[[Category: Montfort, W R.]]
[[Category: Montfort WR]]
[[Category: Rensing, C.]]
[[Category: Rensing C]]
[[Category: Roberts, S A.]]
[[Category: Roberts SA]]
[[Category: Weichsel, A.]]
[[Category: Weichsel A]]
[[Category: Wildner, G F.]]
[[Category: Wildner GF]]
[[Category: Copper]]
[[Category: Multicopper oxidase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:27:27 2008''

Latest revision as of 06:43, 13 August 2026

Copper bound to the Multicopper Oxidase CueO

1n68, resolution 1.70Å

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