|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='5dcr' size='340' side='right'caption='[[5dcr]], [[Resolution|resolution]] 2.11Å' scene=''> | | <StructureSection load='5dcr' size='340' side='right'caption='[[5dcr]], [[Resolution|resolution]] 2.11Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dcr]] is a 1 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=5DCR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DCR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dcr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_kaustophilus_HTA426 Geobacillus kaustophilus HTA426]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DCR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN3:MANGANESE+(III)+ION'>MN3</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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]] 2.108Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hr0|4hr0]], [[4hr4|4hr4]], [[4hr5|4hr5]], [[4xbv|4xbv]], [[4xb9|4xb9]], [[5dco|5dco]], [[4xbw|4xbw]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN3:MANGANESE+(III)+ION'>MN3</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dcr OCA], [https://pdbe.org/5dcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dcr RCSB], [https://www.ebi.ac.uk/pdbsum/5dcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dcr ProSAT]</span></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://proteopedia.org/fgij/fg.htm?mol=5dcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dcr OCA], [http://pdbe.org/5dcr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dcr RCSB], [http://www.ebi.ac.uk/pdbsum/5dcr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dcr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5KW80_GEOKA Q5KW80_GEOKA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 19: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5dcr" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5dcr" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Geoka]] | + | [[Category: Geobacillus kaustophilus HTA426]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribonucleoside-diphosphate reductase]]
| + | [[Category: Griese JJ]] |
| - | [[Category: Griese, J J]] | + | [[Category: Hogbom M]] |
| - | [[Category: Hogbom, M]] | + | |
| - | [[Category: Diiron cofactor]]
| + | |
| - | [[Category: Metalloprotein oxidoreductase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: R2-like ligand-binding oxidase]]
| + | |
| - | [[Category: Ribonucleotide reductase r2 subunit fold]]
| + | |
| Structural highlights
Function
Q5KW80_GEOKA
Publication Abstract from PubMed
Two recently discovered groups of prokaryotic di-metal carboxylate proteins harbor a heterodinuclear Mn/Fe cofactor. These are the class Ic ribonucleotide reductase R2 proteins and a group of oxidases that are found predominantly in pathogens and extremophiles, called R2-like ligand-binding oxidases (R2lox). We have recently shown that the Mn/Fe cofactor of R2lox self-assembles from MnII and FeII in vitro and catalyzes formation of a tyrosine-valine ether crosslink in the protein scaffold [Griese JJ et al. (2013) Proc. Natl. Acad. Sci. USA 110:17189-17194]. Here we present a detailed structural analysis of R2lox in the non-activated, reduced and oxidized resting Mn/Fe- and Fe/Fe-bound states, as well as the non-activated Mn/Mn-bound state. X-ray crystallography and X-ray absorption spectroscopy demonstrate that the active site ligand configuration of R2lox is essentially the same regardless of cofactor composition. Both the Mn/Fe and the diiron cofactor activate oxygen and catalyze formation of the ether crosslink, whereas the dimanganese cluster does not. The structures delineate likely routes for gated oxygen and substrate access to the active site that are controlled by the redox state of the cofactor. These results suggest that oxygen activation proceeds via the same mechanism at the Mn/Fe and Fe/Fe center, and that R2lox proteins might utilize either cofactor in vivo based on metal availability.
Structural Basis for Oxygen Activation at a Heterodinuclear Mn/Fe Cofactor.,Griese JJ, Kositzki R, Schrapers P, Branca RM, Nordstrom A, Lehtio J, Haumann M, Hogbom M J Biol Chem. 2015 Aug 31. pii: jbc.M115.675223. PMID:26324712[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Griese JJ, Kositzki R, Schrapers P, Branca RM, Nordstrom A, Lehtio J, Haumann M, Hogbom M. Structural Basis for Oxygen Activation at a Heterodinuclear Mn/Fe Cofactor. J Biol Chem. 2015 Aug 31. pii: jbc.M115.675223. PMID:26324712 doi:http://dx.doi.org/10.1074/jbc.M115.675223
|
