x-Ray Structure of Streptomyces avermitilis Phospholipase D Reveals a Ca²⁺-Stabilized Expanded Active-Site Cleft Adapted for Phospholipid Binding.

April 30, 2026

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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.

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Reveals molecular mechanisms of phospholipid binding in Streptomyces avermitilis phospholipase D, suggesting applications for enzyme engineering.

-stabilized expanded active site of a PhoD-type PLD and clarify the molecular basis for its phospholipid specificity.

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Yasutake et al. (2026) studied this question.

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