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6f6h
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==R2-like ligand-binding oxidase V72L mutant with aerobically reconstituted Mn/Fe cofactor== | |
| + | <StructureSection load='6f6h' size='340' side='right' caption='[[6f6h]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6f6h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Geoka Geoka]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F6H FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MN3:MANGANESE+(III)+ION'>MN3</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hr0|4hr0]], [[4hr4|4hr4]], [[4hr5|4hr5]], [[4xb9|4xb9]], [[4xbv|4xbv]], [[4xbw|4xbw]], [[5dco|5dco]], [[5dcr|5dcr]], [[5dcs|5dcs]], [[5ekb|5ekb]], [[5omk|5omk]], [[5omj|5omj]], [[6f65|6f65]], [[6f6b|6f6b]], [[6f6c|6f6c]], [[6f6e|6f6e]], [[6f6f|6f6f]], [[6f6g|6f6g]], [[6f6k|6f6k]], [[6f6l|6f6l]], [[6f6m|6f6m]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GK2771 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=235909 GEOKA])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f6h OCA], [http://pdbe.org/6f6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f6h RCSB], [http://www.ebi.ac.uk/pdbsum/6f6h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f6h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | R2-like ligand-binding oxidases contain a dinuclear metal cofactor which can consist either of two iron ions or one manganese and one iron ion, but the heterodinuclear Mn/Fe cofactor is the preferred assembly in the presence of Mn(II) and Fe(II) in vitro. We have previously shown that both types of cofactor are capable of catalyzing formation of a tyrosine-valine ether cross-link in the protein scaffold. Here we demonstrate that Mn/Fe centers catalyze cross-link formation more efficiently than Fe/Fe centers, indicating that the heterodinuclear cofactor is the biologically relevant one. We further explore the chemical potential of the Mn/Fe cofactor by introducing mutations at the cross-linking valine residue. We find that cross-link formation is possible also to the tertiary beta-carbon in an isoleucine, but not to the secondary beta-carbon or tertiary gamma-carbon in a leucine, nor to the primary beta-carbon of an alanine. These results illustrate that the reactivity of the cofactor is highly specific and directed. | ||
| - | + | Ether cross-link formation in the R2-like ligand-binding oxidase.,Griese JJ, Branca RMM, Srinivas V, Hogbom M J Biol Inorg Chem. 2018 Jun 26. pii: 10.1007/s00775-018-1583-3. doi:, 10.1007/s00775-018-1583-3. PMID:29946980<ref>PMID:29946980</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Griese, J | + | <div class="pdbe-citations 6f6h" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Geoka]] | ||
| + | [[Category: Ribonucleoside-diphosphate reductase]] | ||
| + | [[Category: Griese, J J]] | ||
[[Category: Hogbom, M]] | [[Category: Hogbom, M]] | ||
| + | [[Category: Metalloprotein oxidoreductase]] | ||
| + | [[Category: Mn/fe cofactor]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: R2-like ligand-binding oxidase]] | ||
| + | [[Category: Ribonucleotide reductase r2 subunit fold]] | ||
Current revision
R2-like ligand-binding oxidase V72L mutant with aerobically reconstituted Mn/Fe cofactor
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