1c40
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BAR-HEADED GOOSE HEMOGLOBIN (AQUOMET FORM)
OverviewOverview
Haemoglobin from the bar-headed goose (Anser indicus) has higher oxygen, affinity than that from its lowland relatives such as greylag goose (A., anser). The crystal structure of bar-headed goose aquomet haemoglobin was, determined at 2.3 A resolution and compared with the structures of the, goose oxy, human, horse and other avian haemoglobins and the sequences of, other avian haemoglobins. Four amino-acid residues differ between greylag, goose and bar-headed goose haemoglobins, among which Alaalpha119 and, Aspbeta125 in bar-headed goose haemoglobin reduces the contacts between, the alpha(1) and beta(1) subunits compared with Pro and Glu, respectively, and therefore may increase the oxygen affinity by loosening the, alpha(1)beta(1) interface. Compared with human oxy haemoglobin, the, relative orientation of two alphabeta dimers in the bar-headed goose, aquomet and oxy Hbs are rotated by about 4 degrees, indicating a unique, quaternary structural difference from the typical R state. This new 'R(H)', state is probably correlated with the higher oxygen affinity of bar-headed, goose haemoglobin.
About this StructureAbout this Structure
1C40 is a Protein complex structure of sequences from Anser indicus with HEM as ligand. This structure superseeds the now removed PDB entry 1C0H. Full crystallographic information is available from OCA.
ReferenceReference
Avian haemoglobins and structural basis of high affinity for oxygen: structure of bar-headed goose aquomet haemoglobin., Liu XZ, Li SL, Jing H, Liang YH, Hua ZQ, Lu GY, Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):775-83. Epub 2001, May 25. PMID:11375496
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