1T1N
CRYSTAL STRUCTURE OF CARBONMONOXY HEMOGLOBIN
Summary for 1T1N
Entry DOI | 10.2210/pdb1t1n/pdb |
Descriptor | PROTEIN (HEMOGLOBIN), PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (5 entities in total) |
Functional Keywords | oxygen transport, hemoglobin |
Biological source | Trematomus newnesi (dusky notothen) More |
Total number of polymer chains | 2 |
Total formula weight | 33238.70 |
Authors | Mazzarella, L.,Vitagliano, L.,Savino, C.,Zagari, A. (deposition date: 1999-03-05, release date: 1999-04-29, Last modification date: 2024-10-30) |
Primary citation | Mazzarella, L.,D'Avino, R.,di Prisco, G.,Savino, C.,Vitagliano, L.,Moody, P.C.E.,Zagari, A. Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question. J.Mol.Biol., 287:897-906, 1999 Cited by PubMed Abstract: 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. PubMed: 10222199DOI: 10.1006/jmbi.1999.2632 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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