title: Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.
abstract: The three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata has been determined on the basis of 489 interproton and 24 hydrogen-bonding distance restraints supplemented by 23 phi backbone and 21 chi 1 side-chain torsion angle restraints derived from nuclear magnetic resonance (NMR) measurements. A total of 42 structures is calculated by a hybrid metric matrix distance geometry-dynamical simulated annealing approach. Both the backbone and side-chain atom positions are well defined. The average atomic rms difference between the 42 individual SA structures and the mean structure obtained by averaging their coordinates is 0.67 +/- 0.12 A for the backbone atoms and 0.90 +/- 0.17 A for all atoms. The core of the protein is formed by a triple-stranded antiparallel beta-sheet composed of residues 14-16 (strand 1), 30-34 (strand 2), and 37-41 (strand 3) with an additional mini-antiparallel beta-sheet at the N-terminus (residues 6-9). The first and second strands of the triple-stranded antiparallel beta-sheet are connected by a long exposed loop (residues 17-30). A number of side-chain interactions are discussed in light of the structure.
authors.affiliation: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892.
authors.forename: P C
authors.initials: PC
authors.lastname: Driscoll
authors.forename: A M
authors.initials: AM
authors.lastname: Gronenborn
authors.forename: L
authors.initials: L
authors.lastname: Beress
authors.forename: G M
authors.initials: GM
authors.lastname: Clore
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000959:Antihypertensive Agents; D000998:Antiviral Agents; D003064:Cnidarian Venoms; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011522:Protons; D012615:Sea Anemones
chemical_list: D000959:Antihypertensive Agents; D000998:Antiviral Agents; C059796:BDS-I antiviral protein, Anemonia sulcata; D003064:Cnidarian Venoms; D011522:Protons