Three-dimensional reconstruction of the hexagonal bilayer hemoglobin of the hydrothermal vent tube worm Riftia pachyptila by cryoelectron microscopy.
A frozen-hydrated specimen of the V1 hemoglobin of the hydrothermal vent tube worm Riftia pachyptila was observed in the electron microscope and subjected to three-dimensional reconstruction by the method of random conical tilt series. The 3D volume possesses a D6 point-group symmetry. When viewed along its 6-fold axis the vertices of its upper hexagonal layer are 16 degrees 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 3-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 Riftia pachyptyla and of the leech Macrobdella decora look almost perfectly identical.
de Haas
F
F
Groupe d'Analyse Structurale des Antigènes (URA 1334 CNRS), Tours, France.
Zal
F
F
Lallier
F H
FH
Toulmond
A
A
Lamy
J N
JN
D000818:Animals; D015925:Cryopreservation; D006454:Hemoglobins / Q000648:ultrastructure*; D007091:Image Processing, Computer-Assisted / Q000379:methods; D008854:Microscopy, Electron / Q000379:methods; D008958:Models, Molecular; D011077:Polychaeta / Q000737:chemistry*; D011487:Protein Conformation
D006454:Hemoglobins