Data di Pubblicazione:
2005
Citazione:
Structural Studies on Cerebratulus lacteus Mini-Hb K(E10)W and L(G12)A Mutants / M. Nardini, A. Pesce, S. Dewilde, L. Moens, M. Bolognesi. - In: ACTA CRYSTALLOGRAPHICA. SECTION A, FOUNDATIONS OF CRYSTALLOGRAPHY. - ISSN 0108-7673. - A61:(2005), pp. c212-c212. ((Intervento presentato al 20. convegno 20. Congress of the International Union of Crystallography tenutosi a Firenze nel 2005.
Abstract:
A very short hemoglobin (CerHb; 109 amino acids) binds O2 cooperatively in the nerve tissue of the nemertean worm Cerebratulus
lacteus to sustain neural activity during anoxia. The structure of oxygenated wild-type CerHb displays a substantial editing of the globin fold which makes CerHb unique among the known globin fold evolutionary variants.
Here we present the crystal structures of two CerHb mutants:
Lys(E10)Trp (at 2.3 Å resolution) and Leu(G12)Ala (at 1.6 Å
resolution) and its complex with xenon atoms (at 2.3 Å resolution).
The single mutation Lys(E10)Trp, intended to perturb the protein
heme binding, has also a dramatic and unexpected effect on the Hbond
network stabilizing the O2 ligand, and it makes the protein more
susceptible to heme-iron oxidation.
The Leu(G12)Ala mutant and its complex with xenon atoms map
a wide protein matrix tunnel connecting the distal site to a surface
cleft between the E and H helices, thus suggesting a novel ligand
access to heme.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
M. Nardini, A. Pesce, S. Dewilde, L. Moens, M. Bolognesi
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