Structure of the trigonal crystal form of bovine annexin IV

• Published in: Biochemical journal Vol. 329 ( Pt 1); no. 1; pp. 101 - 106
• Main Authors: Zanotti, G, Malpeli, G, Gliubich, F, Folli, C, Stoppini, M, Olivi, L, Savoia, A, Berni, R
• Format: Journal Article
• Language: English
• Published: England 01.01.1998
• Subjects: Amino Acid Sequence; Animals; Annexin A4 - analogs & derivatives; Annexin A4 - chemistry; Annexin A4 - isolation & purification; Cattle; Crystallization; Crystallography, X-Ray; Hydrogen Bonding; Kidney - chemistry; Models, Molecular; Molecular Sequence Data; Phospholipids - metabolism; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj3290101

The structure of a trigonal crystal form of N-terminally truncated [des-(1-9)] bovine annexin IV, an annexin variant that exhibits the distinctive property of binding both phospholipids and carbohydrates in a Ca2+-dependent manner, has been determined at 3 A (0.3 nm) resolution -space group: R3; cell parameters: a=b=118.560 (8) A and c=82.233 (6) A-. The overall structure of annexin IV, crystallized in the absence of Ca2+ ions, is highly homologous to that of the other known members of the annexin family. The trimeric assembly in the trigonal crystals of annexin IV is quite similar to that found previously in non-isomorphous crystals of human, chicken and rat annexin V and to the subunit arrangement in half of the hexamer of hydra annexin XII. Moreover, it resembles that found in two-dimensional crystals of human annexin V bound to phospholipid monolayers. The propensity of several annexins to generate similar trimeric arrays supports the hypothesis that trimeric complexes of such annexins, including annexin IV, may represent the functional units that interact with membranes.