5ker: Difference between revisions
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==Deer mouse recombinant hemoglobin from high altitude species== | ==Deer mouse recombinant hemoglobin from high altitude species== | ||
<StructureSection load='5ker' size='340' side='right' caption='[[5ker]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5ker' size='340' side='right'caption='[[5ker]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ker]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KER OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5ker]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Msb_mamm_74965 Msb mamm 74965]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KER OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KER FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HBA, Hba, HBAT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10042 MSB Mamm 74965]), HBB, HBB-T1, HBB-T2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10042 MSB Mamm 74965])</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=5ker FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ker OCA], [http://pdbe.org/5ker PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ker RCSB], [http://www.ebi.ac.uk/pdbsum/5ker PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ker ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ker" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ker" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Msb mamm 74965]] | |||
[[Category: Inoguchi, N]] | [[Category: Inoguchi, N]] | ||
[[Category: Moriyama, H]] | [[Category: Moriyama, H]] | ||
Revision as of 18:24, 8 July 2020
Deer mouse recombinant hemoglobin from high altitude speciesDeer mouse recombinant hemoglobin from high altitude species
Structural highlights
Publication Abstract from PubMedBACKGROUND: Deer mice (Peromyscus maniculatus) that are native to high altitudes in the Rocky Mountains have evolved hemoglobins with an increased oxygen-binding affinity relative to those of lowland conspecifics. To elucidate the molecular mechanisms responsible for the evolved increase in hemoglobin-oxygen affinity, the crystal structure of the highland hemoglobin variant was solved and compared with the previously reported structure for the lowland variant. RESULTS: Highland hemoglobin yielded at least two crystal types, in which the longest axes were 507 and 230 A. Using the smaller unit cell crystal, the structure was solved at 2.2 A resolution. The asymmetric unit contained two tetrameric hemoglobin molecules. CONCLUSIONS: The analyses revealed that alphaPro50 in the highland hemoglobin variant promoted a stable interaction between alphaHis45 and heme that was not seen in the alphaHis50 lowland variant. The alphaPro50 mutation also altered the nature of atomic contacts at the alpha1beta2/alpha2beta1 intersubunit interfaces. These results demonstrate how affinity-altering changes in intersubunit interactions can be produced by mutations at structurally remote sites. Alteration of the alpha1beta2/alpha2beta1 subunit interface contributes to the increased hemoglobin-oxygen affinity of high-altitude deer mice.,Inoguchi N, Mizuno N, Baba S, Kumasaka T, Natarajan C, Storz JF, Moriyama H PLoS One. 2017 Mar 31;12(3):e0174921. doi: 10.1371/journal.pone.0174921., eCollection 2017. PMID:28362841[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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