3rym

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Current revision (12:40, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3rym' size='340' side='right'caption='[[3rym]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3rym' size='340' side='right'caption='[[3rym]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rym]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RYM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rym]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RYM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 1.7039&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aac|1aac]], [[2ov0|2ov0]], [[3ie9|3ie9]]</div></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=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ami, mauC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741])</td></tr>
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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=3rym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rym OCA], [https://pdbe.org/3rym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rym RCSB], [https://www.ebi.ac.uk/pdbsum/3rym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rym ProSAT]</span></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=3rym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rym OCA], [https://pdbe.org/3rym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rym RCSB], [https://www.ebi.ac.uk/pdbsum/3rym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rym ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE]] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
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[https://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mutation of the axial ligand of the type I copper protein amicyanin from Met to Lys results in a protein that is spectroscopically invisible and redox inactive. M98K amicyanin acts as a competitive inhibitor in the reaction of native amicyanin with methylamine dehydrogenase indicating that the M98K mutation has not affected the affinity for its natural electron donor. The crystal structure of M98K amicyanin reveals that its overall structure is very similar to native amicyanin but that the type I binding site is occupied by zinc. Anomalous difference Fourier maps calculated using the data collected around the absorption edges of copper and zinc confirm the presence of Zn(2+) at the type I site. The Lys98 NZ donates a hydrogen bond to a well-ordered water molecule at the type I site which enhances the ability of Lys98 to provide a ligand for Zn(2+). Attempts to reconstitute M98K apoamicyanin with copper resulted in precipitation of the protein. The fact that the M98K mutation generated such a selective zinc-binding protein was surprising as ligation of zinc by Lys is rare and this ligand set is unique for zinc.
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Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper.,Sukumar N, Choi M, Davidson VL J Inorg Biochem. 2011 Aug 12;105(12):1638-1644. PMID:22071089<ref>PMID:22071089</ref>
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==See Also==
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*[[Amicyanin 3D structures|Amicyanin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rym" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 17741]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Davidson, V L]]
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[[Category: Paracoccus denitrificans]]
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[[Category: Sukumar, N]]
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[[Category: Davidson VL]]
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[[Category: Beta sandwich]]
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[[Category: Sukumar N]]
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[[Category: Electron transport]]
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[[Category: Metal binding]]
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[[Category: Type i blue copper protein]]
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Current revision

Structure of Oxidized M98K mutant of Amicyanin

PDB ID 3rym

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Proteopedia Page Contributors and Editors (what is this?)

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