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The first crystal structure of a phospholipase D
I Leiros1, F Secundo, C Zambonelli
1Department of Chemistry, Faculty of Science, University of Tromso, Norway.
Structure (London, England : 1993)
|June 30, 2000
Summary
The first crystal structure of phospholipase D (PLD) reveals its two-domain fold and active site. This bacterial PLD structure offers insights into related enzymes, including nucleases and toxins.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- The phospholipase D (PLD) superfamily encompasses enzymes critical for phospholipid metabolism, including nucleases, toxins, and viral proteins.
- PLD hydrolyzes phospholipids to phosphatidic acid, a key signaling molecule, and also catalyzes transphosphatidylation reactions.
- Phosphatidic acid plays a significant role in cellular signal transduction pathways.
Purpose of the Study:
- To determine the crystal structure of a bacterial phospholipase D (PLD).
- To elucidate the structural basis for PLD enzymatic activity and its superfamily relationships.
Main Methods:
- X-ray crystallography was employed to determine the structure of a 54 kDa PLD from Streptomyces sp. strain PMF.
- Multiwavelength anomalous dispersion (MAD) phasing was used for initial structure determination at 1.9 Å resolution.
- Refinement of the crystal structure was achieved to a resolution of 1.4 Å.
Main Results:
- The first crystal structure of a bacterial PLD was determined at high resolution (1.4 Å).
- The PLD structure reveals a single polypeptide chain folded into two distinct domains with an active site at their interface.
- The structure supports a conserved superfamily relationship between PLD and other enzymes like bacterial endonucleases.
Conclusions:
- The determined PLD structure provides crucial insights into the structure and function of diverse enzymes within the PLD superfamily.
- This includes bacterial, plant, and mammalian PLDs, as well as enzymes such as cardiolipin synthases, phosphatidylserine synthases, toxins, and endonucleases.
- Common structural features, including phosphodiester binding capability and bi-lobed monomer/dimer activity, are highlighted across these related enzymes.