Structural highlights
Function
[HBB_TRENE] Involved in oxygen transport from gills to the various peripheral tissues.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
As new structural data have become available, somewhat contrasting explanations of the Root effect in fish haemoglobins (Hb) have been provided. Hb 1 of the Antarctic fish Trematomus newnesi has a nearly pH-independent oxygen affinity, in spite of 95 % sequence identity with Hb 1 of Trematomus (previously named Pagothenia) bernacchii that has a strong Root effect. Here, the 2.2 A R-state structure of Trematomus newnesi Hb 1 is presented. The structure is similar to that of Root effect fish Hbs from Spot and T. bernacchii, suggesting that the differences in the pH dependence cannot be related to the modulation of the R-state. In comparison to T. bernacchii Hb 1, the role of the three mutations Thr41 (C6)alpha-->Ile, Ala97 (G3)alpha-->Ser and His41 (C7)beta-->Tyr at the alpha1beta2-interface is discussed.
Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question.,Mazzarella L, D'Avino R, di Prisco G, Savino C, Vitagliano L, Moody PC, Zagari A J Mol Biol. 1999 Apr 16;287(5):897-906. PMID:10222199[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mazzarella L, D'Avino R, di Prisco G, Savino C, Vitagliano L, Moody PC, Zagari A. Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question. J Mol Biol. 1999 Apr 16;287(5):897-906. PMID:10222199 doi:10.1006/jmbi.1999.2632
