5ker: Difference between revisions
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<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 with sequence from [ | <table><tr><td colspan='2'>[[5ker]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Peromyscus_maniculatus Peromyscus maniculatus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5KER FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.202Å</td></tr> | ||
<tr id=' | <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ker FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ker OCA], [https://pdbe.org/5ker PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ker RCSB], [https://www.ebi.ac.uk/pdbsum/5ker PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ker ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A4ZQ87_PERMA A4ZQ87_PERMA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Peromyscus maniculatus]] | ||
[[Category: Inoguchi | [[Category: Inoguchi N]] | ||
[[Category: Moriyama | [[Category: Moriyama H]] | ||
[[Category: Natarajan | [[Category: Natarajan C]] | ||
[[Category: Storz | [[Category: Storz JF]] | ||
Latest revision as of 12:59, 27 September 2023
Deer mouse recombinant hemoglobin from high altitude speciesDeer mouse recombinant hemoglobin from high altitude species
Structural highlights
FunctionPublication 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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