1pf3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1pf3.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1pf3", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1pf3|  PDB=1pf3  |  SCENE=  }}
'''Crystal Strucuture of the M441L mutant of the multicopper oxidase CueO'''


==Crystal Structure of the M441L mutant of the multicopper oxidase CueO==
<StructureSection load='1pf3' size='340' side='right'caption='[[1pf3]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pf3]] 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=1PF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PF3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pf3 OCA], [https://pdbe.org/1pf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pf3 RCSB], [https://www.ebi.ac.uk/pdbsum/1pf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pf3 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/pf/1pf3_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=1pf3 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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1PF3 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=1PF3 OCA].
</div>
<div class="pdbe-citations 1pf3" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Blue copper oxidase CueO 3D structures|Blue copper oxidase CueO 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[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 Sat May  3 05:00:45 2008''

Latest revision as of 06:54, 13 August 2026

Crystal Structure of the M441L mutant of the multicopper oxidase CueO

1pf3, resolution 1.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1pf3&oldid=4476384"