1BDS

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

Summary for 1BDS

• Entry DOI: 10.2210/pdb1bds/pdb
• Descriptor: BDS-I (1 entity in total)
• Functional Keywords: anti-hypertensive, anti-viral protein
• Biological source: Anemonia sulcata (snake-locks sea anemone)
• Cellular location: Secreted : P11494
• Total number of polymer chains: 1
• Total formula weight: 4719.43

Authors

Clore, G.M.,Driscoll, P.C.,Gronenborn, A.M. (deposition date: 1988-11-14, release date: 1989-01-09, Last modification date: 2024-10-30)

Primary citation

Driscoll, P.C.,Gronenborn, A.M.,Beress, L.,Clore, G.M.
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.
Biochemistry, 28:2188-2198, 1989

PubMed 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.

PubMed: 2566326
DOI: 10.1021/bi00431a033

Experimental method

SOLUTION NMR