3g5w: Difference between revisions

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<StructureSection load='3g5w' size='340' side='right'caption='[[3g5w]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3g5w' size='340' side='right'caption='[[3g5w]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3g5w]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G5W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3G5W FirstGlance]. <br>
<table><tr><td colspan='2'>[[3g5w]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G5W FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1O:CU-O+LINKAGE'>C1O</scene>, <scene name='pdbligand=C2O:CU-O-CU+LINKAGE'>C2O</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3g5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g5w OCA], [http://pdbe.org/3g5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g5w RCSB], [http://www.ebi.ac.uk/pdbsum/3g5w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g5w ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1O:CU-O+LINKAGE'>C1O</scene>, <scene name='pdbligand=C2O:CU-O-CU+LINKAGE'>C2O</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3g5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g5w OCA], [https://pdbe.org/3g5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g5w RCSB], [https://www.ebi.ac.uk/pdbsum/3g5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g5w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q82VX3_NITEU Q82VX3_NITEU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3g5w ConSurf].
</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=3g5w ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The two-domain multicopper oxidases are proposed to be key intermediates in the evolution of three-domain multicopper oxidases. A number of two-domain multicopper oxidases have been identified from genome sequences and are classified as type A, type B, or type C on the basis of the predicted location of the type 1 copper center. The crystal structure of blue copper oxidase, a type C two-domain multicopper oxidase from Nitrosomonas europaea, has been determined to 1.9 A resolution. Blue copper oxidase is a trimer, of which each subunit comprises two cupredoxin domains. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The coordination geometry at the trinuclear copper site is consistent with reduction of the copper ions. Although the overall architecture of blue copper oxidase is similar to nitrite reductases, detailed structural alignments show that the fold and domain orientation more closely resemble the three-domain multicopper oxidases. These observations have important implications for the evolution of nitrite reductases and multicopper oxidases.
Crystal structure of a two-domain multicopper oxidase: implications for the evolution of multicopper blue proteins.,Lawton TJ, Sayavedra-Soto LA, Arp DJ, Rosenzweig AC J Biol Chem. 2009 Apr 10;284(15):10174-80. Epub 2009 Feb 17. PMID:19224923<ref>PMID:19224923</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3g5w" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Nitrosomonas europaea]]
[[Category: Nitrosomonas europaea]]
[[Category: Arp, D J]]
[[Category: Arp DJ]]
[[Category: Lawton, T J]]
[[Category: Lawton TJ]]
[[Category: Rosenzweig, A C]]
[[Category: Rosenzweig AC]]
[[Category: Sayavedra-Soto, L A]]
[[Category: Sayavedra-Soto LA]]
[[Category: Laccase]]
[[Category: Metal binding protein]]
[[Category: Multicopper oxidase]]
[[Category: Nitrifier]]
[[Category: Two domain]]

Revision as of 09:52, 21 February 2024

Crystal structure of Blue Copper Oxidase from Nitrosomonas europaea

3g5w, resolution 1.90Å

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