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Three-dimensional reconstruction of the hexagonal bilayer hemoglobin of the hydrothermal vent tube wormRiftia pachyptila by cryoelectron microscopy by de Haas, Felix; Zal, Franck; Lallier, François H.; Toulmond, André; Lamy, Jean N. is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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A frozen-hydrated specimen of the V1 hemoglobin of the hydrothermal vent tube worm Riftia pwhyptila was observed in the electron microscope and subjected to threedimensional reconstruction by the method of random conical tilt series. The 3D volume possesses a D, point-group symmetry. When viewed along its 6-fold axis the vertices of its upper hexagonal layer are 16" clockwise rotated compared to those of the lower layer. A central linker complex is decorated by 12 hollow globular substructures. The linker complex comprises (i) a central hexagonal toroid, (ii) two internal bracelets onto which the hollow globular substructures are built, and (iii) six structures connecting the two hexagonal layers. The hollow globular substructures, related to the dodecamers of globin chains resulting from the dissociation of the hexagonal bilayer hemoglobin, have a local pseudo %fold symmetry and are composed each of three elongated structures visible when the volume is displayed at high threshold. At a resolution of 36 A, the 3D volumes of the hexagonal bilayer hemoglobins of Ri.ftia pachyptyla and of the leech M w r o bdella decora look almost perfectly identical.

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Author

de Haas, Felix; Zal, Franck; Lallier, François H.; Toulmond, André; Lamy, Jean N.

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)