1XXS

Structural insights for fatty acid binding in a Lys49 phospholipase A2: crystal structure of myotoxin II from Bothrops moojeni complexed with stearic acid

Summary for 1XXS

• Entry DOI: 10.2210/pdb1xxs/pdb
• Related: 1GOD 1PA0 1PC9
• Descriptor: Phospholipase A2 homolog 2, SULFATE ION, STEARIC ACID (3 entities in total)
• Functional Keywords: phospholipase a2, stearic acid, dimer interface, fatty acid binding, hydrolase
• Biological source: Bothrops moojeni
• Cellular location: Secreted: Q9I834
• Total number of polymer chains: 2
• Total formula weight: 29859.40

Authors

Watanabe, L.,Soares, A.M.,Ward, R.J.,Fontes, M.R.,Arni, R.K. (deposition date: 2004-11-08, release date: 2005-03-29, Last modification date: 2024-04-03)

Primary citation

Watanabe, L.,Soares, A.M.,Ward, R.J.,Fontes, M.R.,Arni, R.K.
Structural insights for fatty acid binding in a Lys49-phospholipase A(2): crystal structure of myotoxin II from Bothrops moojeni complexed with stearic acid
Biochimie, 87:161-167, 2005

PubMed Abstract: The crystal structure of dimeric Lys49-phospholipase A2 myotoxin-II from Bothrops moojeni (MjTX-II) co-crystallized with stearic acid (C(18)H(36)O(2)) has been determined at a resolution of 1.8 A. The electron density maps permitted the unambiguous inclusion of six stearic acid molecules in the refinement. Two stearic acid molecules could be located in the substrate-binding cleft of each monomer in positions, which favor the interaction of their carboxyl groups with active site residues. The way of binding of stearic acids to this Lys49-PLA(2)s is analogous to phospholipids and transition state analogues to catalytically active PLA(2)s. Two additional stearic acid molecules were located at the dimer interface region, defining a hitherto unidentified acyl-binding site on the protein surface. The strictly conserved Lys122 for Lys49-PLA(2)s may play a fundamental role for stabilization of legend-protein complex. The comparison of MjTX-II/satiric acid complex with other Lys-PLA(2)s structures whose putative fatty acids were located at their active site is also analysed. Molecular details of the stearic acid/protein interactions provide insights to binding in group I/II PLA(2)s, and to the possible interactions of Lys49-PLA(2)s with target membranes.

PubMed: 15760708
DOI: 10.1016/j.biochi.2004.11.005

Experimental method

X-RAY DIFFRACTION (1.8 Å)