1AEI

CRYSTAL STRUCTURE OF THE ANNEXIN XII HEXAMER

Summary for 1AEI

• Entry DOI: 10.2210/pdb1aei/pdb
• Descriptor: ANNEXIN XII, CALCIUM ION (2 entities in total)
• Functional Keywords: calcium/phospholipid-binding, annexin, calcium, phospholipid, calcium-phospholipid-binding complex
• Biological source: Hydra vulgaris
• Total number of polymer chains: 6
• Total formula weight: 211108.71

Authors

Luecke, H.,Chang, B.T.,Mailliard, W.S.,Schlaepfer, D.D.,Haigler, H.T. (deposition date: 1995-09-23, release date: 1997-08-20, Last modification date: 2024-04-03)

Primary citation

Luecke, H.,Chang, B.T.,Mailliard, W.S.,Schlaepfer, D.D.,Haigler, H.T.
Crystal structure of the annexin XII hexamer and implications for bilayer insertion.
Nature, 378:512-515, 1995

PubMed Abstract: Annexins are a family of calcium- and phospholipid-binding proteins implicated in a number of biological processes including membrane fusion and ion channel formation. The crystal structure of the annexin XII hexamer, refined at 2.8 A resolution, forms a concave disk with 3-2 symmetry, about 100 A in diameter and 70 A thick with a central hydrophilic pore. Six intermolecular Ca2+ ions are involved in hexamer formation. An additional 18 Ca2+ ions are located on the perimeter of the disk, accessible only from the side of the hexameric disk. On the basis of the hexamer structure we propose here a new mode of protein-phospholipid bilayer interaction that is distinct from the hydrophobic insertion of typical membrane proteins. This speculative model postulates the Ca(2+)-dependent insertion of the hydrophilic annexin XII hexamer into phospholipid bilayers with local reorientation of the bilayer phospholipids.

PubMed: 7477411
DOI: 10.1038/378512a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)