1w6l

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[[Image:1w6l.gif|left|200px]]
 
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==3D structure of CotA incubated with CuCl2==
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The line below this paragraph, containing "STRUCTURE_1w6l", creates the "Structure Box" on the page.
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<StructureSection load='1w6l' size='340' side='right'caption='[[1w6l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1w6l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W6L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
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{{STRUCTURE_1w6l| PDB=1w6l | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6l OCA], [https://pdbe.org/1w6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w6l RCSB], [https://www.ebi.ac.uk/pdbsum/1w6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w6l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/COTA_BACSU COTA_BACSU] Involved in brown pigmentation during sporogenesis.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/1w6l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1w6l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The multi-copper oxidases oxidise substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. The precise mechanism of this reduction has been unclear, but recent X-ray structural studies using the CotA endospore coat protein from Bacillus subtilis have given further insights into the principal stages. It is proposed that the mechanism involves binding of the dioxygen into the trinuclear centre so that it is sited approximately symmetrically between the two type 3 copper ions with one oxygen atom close to the type 2 copper ion. Further stages involve the formation of a peroxide intermediate and following the splitting of this intermediate, the migration of the hydroxide moieties towards the solvent exit channel. The migration steps are likely to involve a movement of the type 2 copper ion and its environment. Details of a putative mechanism are described herein based both on structures already reported in the literature and on structures of the CotA protein in the oxidised and reduced states and with the addition of peroxide and the inhibitor, azide.
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'''3D STRUCTURE OF COTA INCUBATED WITH CUCL2'''
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Dioxygen reduction by multi-copper oxidases; a structural perspective.,Bento I, Martins LO, Gato Lopes G, Armenia Carrondo M, Lindley PF Dalton Trans. 2005 Nov 7;(21):3507-13. Epub 2005 Sep 27. PMID:16234932<ref>PMID:16234932</ref>
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==Overview==
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The multi-copper oxidases oxidise substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. The precise mechanism of this reduction has been unclear, but recent X-ray structural studies using the CotA endospore coat protein from Bacillus subtilis have given further insights into the principal stages. It is proposed that the mechanism involves binding of the dioxygen into the trinuclear centre so that it is sited approximately symmetrically between the two type 3 copper ions with one oxygen atom close to the type 2 copper ion. Further stages involve the formation of a peroxide intermediate and following the splitting of this intermediate, the migration of the hydroxide moieties towards the solvent exit channel. The migration steps are likely to involve a movement of the type 2 copper ion and its environment. Details of a putative mechanism are described herein based both on structures already reported in the literature and on structures of the CotA protein in the oxidised and reduced states and with the addition of peroxide and the inhibitor, azide.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1W6L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6L OCA].
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</div>
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<div class="pdbe-citations 1w6l" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Dioxygen reduction by multi-copper oxidases; a structural perspective., Bento I, Martins LO, Gato Lopes G, Armenia Carrondo M, Lindley PF, Dalton Trans. 2005 Nov 7;(21):3507-13. Epub 2005 Sep 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16234932 16234932]
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*[[Laccase|Laccase]]
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*[[Laccase 3D structures|Laccase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bento, I.]]
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[[Category: Bento I]]
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[[Category: Carrondo, M A.]]
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[[Category: Carrondo MA]]
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[[Category: Lindley, P F.]]
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[[Category: Lindley PF]]
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[[Category: Lopes, G G.]]
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[[Category: Lopes GG]]
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[[Category: Martins, L O.]]
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[[Category: Martins LO]]
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[[Category: Copper]]
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[[Category: Laccase]]
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[[Category: Multicopper-oxidase]]
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[[Category: Oxidase]]
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[[Category: Oxygen reduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:13:34 2008''
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Current revision

3D structure of CotA incubated with CuCl2

PDB ID 1w6l

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