3VRG

The crystal structure of hemoglobin from woolly mammoth in the met form

Summary for 3VRG

• Entry DOI: 10.2210/pdb3vrg/pdb
• Related: 3VFE 3VFF
• Descriptor: Hemoglobin subunit alpha, Hemoglobin subunit beta/delta hybrid, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: woolly mammoth hemoglobin, oxygen transport, oxygen storage/transport
• Biological source: Mammuthus primigenius (mammoth); More
• Total number of polymer chains: 2
• Total formula weight: 33144.11

Authors

Noguchi, H.,Campbell, K.L.,Ho, C.,Park, S.-Y.,Tame, J.R.H. (deposition date: 2012-04-09, release date: 2012-11-07, Last modification date: 2023-11-08)

Primary citation

Noguchi, H.,Campbell, K.L.,Ho, C.,Unzai, S.,Park, S.-Y.,Tame, J.R.H.
Structures of haemoglobin from woolly mammoth in liganded and unliganded states.
Acta Crystallogr.,Sect.D, 68:1441-1449, 2012

PubMed Abstract: The haemoglobin (Hb) of the extinct woolly mammoth has been recreated using recombinant genes expressed in Escherichia coli. The globin gene sequences were previously determined using DNA recovered from frozen cadavers. Although highly similar to the Hb of existing elephants, the woolly mammoth protein shows rather different responses to chloride ions and temperature. In particular, the heat of oxygenation is found to be much lower in mammoth Hb, which appears to be an adaptation to the harsh high-latitude climates of the Pleistocene Ice Ages and has been linked to heightened sensitivity of the mammoth protein to protons, chloride ions and organic phosphates relative to that of Asian elephants. To elucidate the structural basis for the altered homotropic and heterotropic effects, the crystal structures of mammoth Hb have been determined in the deoxy, carbonmonoxy and aquo-met forms. These models, which are the first structures of Hb from an extinct species, show many features reminiscent of human Hb, but underline how the delicate control of oxygen affinity relies on much more than simple overall quaternary-structure changes.

PubMed: 23090393
DOI: 10.1107/S0907444912029459

Experimental method

X-RAY DIFFRACTION (1.5 Å)