1t1n
From Proteopedia
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CRYSTAL STRUCTURE OF CARBONMONOXY HEMOGLOBIN
Overview
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.
About this Structure
1T1N is a Protein complex structure of sequences from Trematomus newnesi with , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:08:56 2008
Categories: Protein complex | Trematomus newnesi | Mazzarella, L. | Savino, C. | Vitagliano, L. | Zagari, A. | ACE | CMO | HEM | Hemoglobin | Oxygen transport
