6f6c: Difference between revisions
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New page: '''Unreleased structure''' The entry 6f6c is ON HOLD until Paper Publication Authors: Griese, J.J., Hogbom, M. Description: R2-like ligand-binding oxidase V72A mutant with aerobically ... |
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==R2-like ligand-binding oxidase V72A mutant with aerobically reconstituted Mn/Fe cofactor== | |||
<StructureSection load='6f6c' size='340' side='right' caption='[[6f6c]], [[Resolution|resolution]] 1.77Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f6c]] 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=6F6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F6C 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]], [[6f6e|6f6e]], [[6f6f|6f6f]], [[6f6g|6f6g]], [[6f6h|6f6h]], [[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=6f6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f6c OCA], [http://pdbe.org/6f6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f6c RCSB], [http://www.ebi.ac.uk/pdbsum/6f6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f6c 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 6f6c" 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]] | |||
Latest revision as of 09:17, 11 July 2018
R2-like ligand-binding oxidase V72A mutant with aerobically reconstituted Mn/Fe cofactorR2-like ligand-binding oxidase V72A mutant with aerobically reconstituted Mn/Fe cofactor
Structural highlights
Publication Abstract from PubMedR2-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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