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| | <StructureSection load='6qk0' size='340' side='right'caption='[[6qk0]], [[Resolution|resolution]] 2.09Å' scene=''> | | <StructureSection load='6qk0' size='340' side='right'caption='[[6qk0]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qk0]] 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=6QK0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QK0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qk0]] is a 2 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=6QK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QK0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.091Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=6qk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qk0 OCA], [https://pdbe.org/6qk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qk0 RCSB], [https://www.ebi.ac.uk/pdbsum/6qk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qk0 ProSAT]</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=6qk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qk0 OCA], [http://pdbe.org/6qk0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qk0 RCSB], [http://www.ebi.ac.uk/pdbsum/6qk0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qk0 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 == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6qk0" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6qk0" 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: Metalloprotein oxidoreductase]]
| + | |
| - | [[Category: Mn/fe cofactor]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: R2-like ligand-binding oxidase]]
| + | |
| - | [[Category: Ribonucleotide reductase r2 subunit fold]]
| + | |
| Structural highlights
Function
Q5KW80_GEOKA
Publication Abstract from PubMed
Heterobimetallic Mn/Fe proteins represent a new cofactor paradigm in bioinorganic chemistry and pose countless outstanding questions. The assembly of the active site defies common chemical convention by contradicting the Irving-Williams series, while the scope of reactivity remains unexplored. In this work, the assembly and C-H bond activation process in the Mn/Fe R2-like ligand-binding oxidase (R2lox) protein is investigated using a suite of biophysical techniques, including time-resolved optical spectroscopy, global kinetic modeling, X-ray crystallography, electron paramagnetic resonance spectroscopy, protein electrochemistry, and mass spectrometry. Selective metal binding is found to be under thermodynamic control, with the binding sites within the apo-protein exhibiting greater Mn(II) affinity than Fe(II) affinity. The comprehensive analysis of structure and reactivity of wild-type R2lox and targeted primary and secondary sphere mutants indicate that the efficiency of C-H bond activation directly correlates with the Mn/Fe cofactor reduction potentials and is inversely related to divalent metal binding affinity. These findings suggest the R2lox active site is precisely tuned for achieving both selective heterobimetallic binding and high levels of reactivity and offer a mechanism to examine the means by which proteins achieve appropriate metal incorporation.
Key Structural Motifs Balance Metal Binding and Oxidative Reactivity in a Heterobimetallic Mn/Fe Protein.,Kisgeropoulos EC, Griese JJ, Smith ZR, Branca RMM, Schneider CR, Hogbom M, Shafaat HS J Am Chem Soc. 2020 Mar 18;142(11):5338-5354. doi: 10.1021/jacs.0c00333. Epub, 2020 Mar 9. PMID:32062969[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kisgeropoulos EC, Griese JJ, Smith ZR, Branca RMM, Schneider CR, Hogbom M, Shafaat HS. Key Structural Motifs Balance Metal Binding and Oxidative Reactivity in a Heterobimetallic Mn/Fe Protein. J Am Chem Soc. 2020 Mar 18;142(11):5338-5354. doi: 10.1021/jacs.0c00333. Epub, 2020 Mar 9. PMID:32062969 doi:http://dx.doi.org/10.1021/jacs.0c00333
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