x-Ray Structure of Streptomyces avermitilis Phospholipase D Reveals a Ca2+-Stabilized Expanded Active-Site Cleft Adapted for Phospholipid Binding. | Synapse
May 3, 2026
x-Ray Structure of Streptomyces avermitilis Phospholipase D Reveals a Ca2+-Stabilized Expanded Active-Site Cleft Adapted for Phospholipid Binding.
Key Points
The research aims to understand the molecular structure of phospholipase D and its binding affinity for phospholipids.
Conducted X-ray crystallography to determine the structure of phospholipase D from Streptomyces avermitilis.
Analyzed the active-site cleft and identified stabilization mechanisms by calcium ions.
Characterized phospholipid specificity through structural insights.
The expanded active-site cleft stabilizes phospholipid binding through calcium ion interactions.
Structural data revealed key mechanisms underlying specificity for different phospholipid types.
Abstract
-stabilized expanded active site of a PhoD-type PLD and clarify the molecular basis for its phospholipid specificity.