Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question.
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.
Mazzarella
L
L
Centro di Studio di Biocristallografia, CNR, Napoli, Italy. mazarrella@chemna.dichi.unina.it
D'Avino
R
R
di Prisco
G
G
Savino
C
C
Vitagliano
L
L
Moody
P C
PC
Zagari
A
A
D000818:Animals; D018360:Crystallography, X-Ray; D005399:Fishes / Q000097:blood*; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D006454:Hemoglobins