5KER

Deer mouse recombinant hemoglobin from high altitude species

Summary for 5KER

• Entry DOI: 10.2210/pdb5ker/pdb
• Descriptor: Alpha-globin, Beta globin, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: oxygen-transport, transport protein
• Biological source: Peromyscus maniculatus (North American deer mouse); More
• Total number of polymer chains: 8
• Total formula weight: 127652.64

Authors

Inoguchi, N.,Natarajan, C.,Storz, J.F.,Moriyama, H. (deposition date: 2016-06-10, release date: 2017-04-05, Last modification date: 2023-09-27)

Primary citation

Inoguchi, N.,Mizuno, N.,Baba, S.,Kumasaka, T.,Natarajan, C.,Storz, J.F.,Moriyama, H.
Alteration of the alpha 1 beta 2/ alpha 2 beta 1 subunit interface contributes to the increased hemoglobin-oxygen affinity of high-altitude deer mice.
PLoS ONE, 12:e0174921-e0174921, 2017

PubMed Abstract: 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.

PubMed: 28362841
DOI: 10.1371/journal.pone.0174921

Experimental method

X-RAY DIFFRACTION (2.202 Å)