1C40

BAR-HEADED GOOSE HEMOGLOBIN (AQUOMET FORM)

Replaces:  1C0H

Summary for 1C40

• Entry DOI: 10.2210/pdb1c40/pdb
• Descriptor: PROTEIN (HEMOGLOBIN (ALPHA CHAIN)), PROTEIN (HEMOGLOBIN (BETA CHAIN)), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: oxygen transport, heme, respiratory protein, erythrocyte, oxygen storage/ transport, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Anser indicus (bar-headed goose); More
• Total number of polymer chains: 2
• Total formula weight: 32907.53

Authors

Li, S.,Liu, X.,Jing, H.,Hua, Z.,Zhang, R.,Lu, G. (deposition date: 1999-08-03, release date: 1999-08-09, Last modification date: 2023-08-09)

Primary citation

Liu, X.Z.,Li, S.L.,Jing, H.,Liang, Y.H.,Hua, Z.Q.,Lu, G.Y.
Avian haemoglobins and structural basis of high affinity for oxygen: structure of bar-headed goose aquomet haemoglobin.
Acta Crystallogr.,Sect.D, 57:775-783, 2001

PubMed Abstract: 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.

PubMed: 11375496
DOI: 10.1107/S0907444901004243

Experimental method

X-RAY DIFFRACTION (2.3 Å)