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| <StructureSection load='7dgl' size='340' side='right'caption='[[7dgl]], [[Resolution|resolution]] 1.91Å' scene=''> | | <StructureSection load='7dgl' size='340' side='right'caption='[[7dgl]], [[Resolution|resolution]] 1.91Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7dgl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DGL FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DGL FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</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]] 1.91Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene></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=7dgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dgl OCA], [https://pdbe.org/7dgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dgl RCSB], [https://www.ebi.ac.uk/pdbsum/7dgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dgl 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=7dgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dgl OCA], [https://pdbe.org/7dgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dgl RCSB], [https://www.ebi.ac.uk/pdbsum/7dgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dgl ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
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| [[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The metal active site is precisely designed in metalloproteins. Here we applied 3D domain swapping, a phenomenon in which a partial protein structure is exchanged between molecules, to introduce metal sites in proteins. We designed multiple metal-binding sites specific to domain-swapped myoglobin (Mb) with His mutation. Stable dimeric Mbs with metal-binding sites were obtained by shifting the His position and introducing two Ala residues in the hinge region (K78H/G80A/H82A and K79H/G80A/H81A Mbs). The absorption and circular dichroism spectra of the monomer and dimer of K78H/G80A/H82A and K79H/G80A/H81A Mbs were similar to the corresponding spectra, respectively, of wild-type Mb. No negative peak due to dimer-to-monomer dissociation was observed below the denaturation temperature in the differential scanning calorimetry thermograms of K78H/G80A/H82A and K79H/G80A/H81A Mbs, whereas the dimer dissociates into monomers at 68 degrees C for wild-type Mb. These results show that the two mutants were stable in the dimer state. Metal ions bound to the metal-binding sites containing the introduced His in the domain-swapped Mb dimers. Co(2+)-bound and Ni(2+)-bound K78H/G80A/H82A Mb exhibited octahedral metal-coordination structures, where His78, His81, Glu85, and three H2O/OH(-) molecules coordinated to the metal ion. On the other hand, Co(2+)-bound and Zn(2+)-bound K79H/G80A/H81A Mb exhibited tetrahedral metal-coordination structures, where His79, His82, Asp141, and a H2O/OH(-) molecule coordinated to the metal ion. The Co(2+)-bound site exists deep inside the protein in the K79H/G80A/H81A Mb dimer, which may allow the unique tetrahedral coordination for the Co(2+) ion. These results show that we can utilize domain swapping to construct artificial metalloproteins.
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| Rational design of metal-binding sites in domain-swapped myoglobin dimers.,Nagao S, Idomoto A, Shibata N, Higuchi Y, Hirota S J Inorg Biochem. 2021 Jan 28;217:111374. doi: 10.1016/j.jinorgbio.2021.111374. PMID:33578251<ref>PMID:33578251</ref>
| | ==See Also== |
| | | *[[Myoglobin 3D structures|Myoglobin 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7dgl" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Equus caballus]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Higuchi, Y]] | | [[Category: Higuchi Y]] |
| [[Category: Hirota, S]] | | [[Category: Hirota S]] |
| [[Category: Idomoto, A]] | | [[Category: Idomoto A]] |
| [[Category: Nagao, S]] | | [[Category: Nagao S]] |
| [[Category: Shibata, N]] | | [[Category: Shibata N]] |
| [[Category: Oxygen binding]]
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| [[Category: Oxygen storage]]
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