7v5r: Difference between revisions

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==The dimeric structure of G80A/H81A/L137D myoglobin==
==The dimeric structure of G80A/H81A/L137D myoglobin==
<StructureSection load='7v5r' size='340' side='right'caption='[[7v5r]]' scene=''>
<StructureSection load='7v5r' size='340' side='right'caption='[[7v5r]], [[Resolution|resolution]] 1.39&Aring;' 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=7V5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V5R FirstGlance]. <br>
<table><tr><td colspan='2'>[[7v5r]] 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=7V5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V5R FirstGlance]. <br>
</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=7v5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v5r OCA], [https://pdbe.org/7v5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v5r RCSB], [https://www.ebi.ac.uk/pdbsum/7v5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v5r ProSAT]</span></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]] 1.39&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7v5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v5r OCA], [https://pdbe.org/7v5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v5r RCSB], [https://www.ebi.ac.uk/pdbsum/7v5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v5r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://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 ==
Various factors, such as helical propensity and hydrogen bonds, control protein structures. A frequently used model protein, myoglobin (Mb), can perform 3D domain swapping, in which the loop at the hinge region is converted to a helical structure in the dimer. We have previously succeeded in obtaining monomer-dimer equilibrium in the native state by introducing a high alpha-helical propensity residue, Ala, to the hinge region. In this study, we focused on another factor that governs the protein structure, hydrogen bonding. X-ray crystal structures and thermodynamic studies showed that the myoglobin dimer was stabilized over the monomer when keeping His82 to interact with Lys79 and Asp141 through water moleclues and mutating Leu137, which was located close to the H-bond network at the dimer hinge region, to a hydrophilic amino acid (Glu or Asp). Molecular dynamics simulation studies confirmed that the number of H-bonds increased and the alpha-helices at the hinge region became more rigid for mutants with a tighter H-bond network, supporting the hypothesis that the myoglobin dimer is stabilized when the H-bond network at the hinge region is enhanced. This demonstrates the importance and utility of hydrogen bonds for designing a protein dimer from its monomer with 3D domain swapping.
Experimental and theoretical study on converting myoglobin into a stable domain-swapped dimer by utilizing a tight hydrogen bond network at the hinge region.,Xie C, Shimoyama H, Yamanaka M, Nagao S, Komori H, Shibata N, Higuchi Y, Shigeta Y, Hirota S RSC Adv. 2021 Nov 23;11(59):37604-37611. doi: 10.1039/d1ra06888a. eCollection , 2021 Nov 17. PMID:35496441<ref>PMID:35496441</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7v5r" style="background-color:#fffaf0;"></div>
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Equus caballus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Xie, C, Komori, H, Hirota, S]]
[[Category: Hirota S]]
[[Category: Komori H]]
[[Category: Xie C]]

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