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Structural interpretation of the amino acid sequence of a second domain from the Artemia covalent polymer globin

par Moens, Luc;Van Hauwaert, Marie Louise;De Smet, Koen K.A.;Ver Donck, Kris;Van de peer, Yves;Van Beeumen, Jozef;Wodak, Shoshana ;Alard, Philippe ;Trotman, Clive
Référence The Journal of biological chemistry, 265, 24, page (14285-14291)
Publication Publié, 1990-08

Article révisé par les pairs

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Résumé :

Artemia has a complex extracellular hemoglobin of Mr 260,000 comprising two globin chains (Mr 130,000) each of which is a polymer of eight covalently linked domains of Mr 16,000. The primary structure of this polymeric globin was studied to understand how globin folded domains are ordered within a globin chain and, in turn, how the latter associate into a functional hemoglobin molecule. Here we report the amino acid sequence of a second domain, E7 (Mr 16,081, excluding the heme), and interpretations of sequence data by computer-assisted alignment and modeling. This clearly shows that, as with domain E1 (Moens, L., Van Hauwaert, M.-L., De Smet, K., Geelen, D., Verpooten, G., Van Beeumen, J., Wodak, S., Alard, P., & Trotman, C. (1988) J. Biol. Chem. 263, 4679-4685), domain E7 is compatible with a globin folded structure of the β-type chain. Several specific differences of domains E7 and E1 from the classic globins are identified. They possibly can be interpreted in terms of specific requirements for a double octameric functional molecule.