Sub-domain structure of lipid-bound annexin-V resolved by electron image analysis.
Two-dimensional crystals of annexin-V bound to lipid layers containing dioleoylphosphatidylserine have been obtained in the presence of Ca2+. The crystals diffract to 20 A resolution and have the symmetry of the plane group p3 (unit cell dimensions: a = b = 94 A, gamma = 120 degrees). Electron image analysis revealed that the crystals are composed of trimers of annexin-V forming triskelion-like motifs. Each annexin-V molecule has a characteristic elongated shape, about 65 A by 20 A, when observed perpendicularly to the crystal plane. It is composed of two staggered domains of similar size, about 40 A by 20 A. Both domains are made of two sub-domains. The present data suggest that the four resolved sub-domains represent the folding units corresponding to the four 70 amino acid repeating segments characteristic of all annexins.
Mosser
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G
Laboratoire de Génétique Moléculaire des Eucaryotes CNRS, Unité 184 de Biologie Moléculaire et de Génie Génétique INSERM, Institut de Chimie Biologique, Faculté de Médecine, Strasbourg, France.
Ravanat
C
C
Freyssinet
J M
JM
Brisson
A
A
D017304:Annexin A5; D002118:Calcium; D002135:Calcium-Binding Proteins / Q000648:ultrastructure*; D003461:Crystallography; D005583:Fourier Analysis; D006801:Humans; D008055:Lipids; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000648:ultrastructure*; D008854:Microscopy, Electron / Q000379:methods; D010713:Phosphatidylcholines; D010718:Phosphatidylserines
D017304:Annexin A5; D002135:Calcium-Binding Proteins; D008055:Lipids; D046911:Macromolecular Substances; D008565:Membrane Proteins; D010713:Phosphatidylcholines; D010718:Phosphatidylserines; C017251:1,2-oleoylphosphatidylcholine; D002118:Calcium