6ls8: Difference between revisions
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==The monomeric structure of G80A/H81A/H82A myoglobin== | ==The monomeric structure of G80A/H81A/H82A myoglobin== | ||
<StructureSection load='6ls8' size='340' side='right'caption='[[6ls8]]' scene=''> | <StructureSection load='6ls8' size='340' side='right'caption='[[6ls8]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LS8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LS8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ls8]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LS8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LS8 FirstGlance]. <br> | ||
</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=6ls8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ls8 OCA], [http://pdbe.org/6ls8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ls8 RCSB], [http://www.ebi.ac.uk/pdbsum/6ls8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ls8 ProSAT]</span></td></tr> | </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></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=6ls8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ls8 OCA], [http://pdbe.org/6ls8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ls8 RCSB], [http://www.ebi.ac.uk/pdbsum/6ls8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ls8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Domain swapping is an exception to Anfinsen's dogma, and more than one structure can be produced from the same amino acid sequence by domain swapping. We have previously shown that myoglobin (Mb) can form a domain-swapped dimer in which the hinge region is converted to a helical structure. In this study, we showed that domain-swapped dimerization of Mb was achieved by a single Ala mutation of Gly at position 80. Multiple Ala mutations at positions 81 and 82 in addition to position 80 facilitated dimerization of Mb by stabilization of the dimeric states. Domain swapping tendencies correlated well with the helical propensity of the mutated residue in a series of Mb mutants with amino acids introduced to the hinge region. These findings demonstrate that a single mutation in the hinge loop to modify helical propensity can control oligomer formation, providing new ideas to create high-order protein oligomers using domain swapping. | |||
Thermodynamic Control of Domain Swapping by Modulating the Helical Propensity in the Hinge Region of Myoglobin.,Nagao S, Suda A, Kobayashi H, Shibata N, Higuchi Y, Hirota S Chem Asian J. 2020 Apr 24. doi: 10.1002/asia.202000307. PMID:32329228<ref>PMID:32329228</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ls8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Equus caballus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Higuchi Y]] | [[Category: Higuchi, Y]] | ||
[[Category: Hirota S]] | [[Category: Hirota, S]] | ||
[[Category: Kobayashi H]] | [[Category: Kobayashi, H]] | ||
[[Category: Nagao S]] | [[Category: Nagao, S]] | ||
[[Category: Shibata N]] | [[Category: Shibata, N]] | ||
[[Category: Suda A]] | [[Category: Suda, A]] | ||
[[Category: Oxygen binding]] | |||
[[Category: Oxygen storage]] | |||
Revision as of 13:34, 17 June 2020
The monomeric structure of G80A/H81A/H82A myoglobinThe monomeric structure of G80A/H81A/H82A myoglobin
Structural highlights
Function[MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Publication Abstract from PubMedDomain swapping is an exception to Anfinsen's dogma, and more than one structure can be produced from the same amino acid sequence by domain swapping. We have previously shown that myoglobin (Mb) can form a domain-swapped dimer in which the hinge region is converted to a helical structure. In this study, we showed that domain-swapped dimerization of Mb was achieved by a single Ala mutation of Gly at position 80. Multiple Ala mutations at positions 81 and 82 in addition to position 80 facilitated dimerization of Mb by stabilization of the dimeric states. Domain swapping tendencies correlated well with the helical propensity of the mutated residue in a series of Mb mutants with amino acids introduced to the hinge region. These findings demonstrate that a single mutation in the hinge loop to modify helical propensity can control oligomer formation, providing new ideas to create high-order protein oligomers using domain swapping. Thermodynamic Control of Domain Swapping by Modulating the Helical Propensity in the Hinge Region of Myoglobin.,Nagao S, Suda A, Kobayashi H, Shibata N, Higuchi Y, Hirota S Chem Asian J. 2020 Apr 24. doi: 10.1002/asia.202000307. PMID:32329228[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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