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Type: Artigo
Title: The structure of the giant haemoglobin from glossoscolex paulistus
Author: Ruggiero Bachega, Jose Fernando
Maluf, Fernando Vasconcelos
Andi, Babak
Pereira, Humberto D'Muniz
Carazzollea, Marcelo Falsarella
Orville, Allen M.
Tabak, Marcel
Brandao-Neto, Jose
Garratt, Richard Charles
Reboredo, Eduardo Horjales
Abstract: The sequences of all seven polypeptide chains from the giant haemoglobin of the free-living earthworm Glossoscolex paulistus (HbGp) are reported together with the three-dimensional structure of the 3.6 MDa complex which they form. The refinement of the full particle, which has been solved at 3.2 angstrom resolution, the highest resolution reported to date for a hexagonal bilayer haemoglobin composed of 12 protomers, is reported. This has allowed a more detailed description of the contacts between subunits which are essential for particle stability. Interpretation of features in the electron-density maps suggests the presence of metal-binding sites (probably Zn2+ and Ca2+) and glycosylation sites, some of which have not been reported previously. The former appear to be important for the integrity of the particle. The crystal structure of the isolated d chain (d-HbGp) at 2.1 angstrom resolution shows different interchain contacts between d monomers compared with those observed in the full particle. Instead of forming trimers, as seen in the complex, the isolated d chains associate to form dimers across a crystallographic twofold axis. These observations eliminate the possibility that trimers form spontaneously in solution as intermediates during the formation of the dodecameric globin cap and contribute to understanding of the possible ways in which the particle self-assembles
Subject: Hemoglobinas
Country: Estados Unidos
Editor: Wiley
Rights: Fechado
Identifier DOI: 10.1107/S1399004715005453
Date Issue: 2015
Appears in Collections:IB - Artigos e Outros Documentos

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