The first crystal structure of a phospholipase D

  • Leiros I
  • Secundo F
  • Zambonelli C
 et al. 
  • 21

    Readers

    Mendeley users who have this article in their library.
  • 115

    Citations

    Citations of this article.

Abstract

Background: The phospholipase D (PLD) superfamily includes enzymes that are involved in phospholipid metabolism, nucleases, toxins and virus envelope proteins of unknown function. PLD hydrolyzes the terminal phosphodiester bond of phospholipids to phosphatidic acid and a hydrophilic constituent. Phosphatidic acid is a compound that is heavily involved in signal transduction. PLD also catalyses a transphosphatidylation reaction in the presence of phosphatidylcholine and a short-chained primary or secondary alcohol. Results: The first crystal structure of a 54 kDa PLD has been determined to 1.9 Å resolution using the multiwavelength anomalous dispersion (MAD) method on a single WO4ion and refined to 1.4 Å resolution. PLD from the bacterial source Streptomyces sp. strain PMF consists of a single polypeptide chain that is folded into two domains. An active site is located at the interface between these domains. The presented structure supports the proposed superfamily relationship with the published structure of the 16 kDa endonuclease from Salmonella typhimurium. Conclusions: The structure of PLD provides insight into the structure and mode of action of not only bacterial, plant and mammalian PLDs, but also of a variety of enzymes as diverse as cardiolipin synthases, phosphatidylserine synthases, toxins, endonucleases, as well as poxvirus envelope proteins having a so far unknown function. The common features of these enzymes are that they can bind to a phosphodiester moiety, and that most of these enzymes are active as bi-lobed monomers or dimers.

Author-supplied keywords

  • Multiwavelength anomalous dispersion (MAD)
  • Phosphate-inhibition, phospholipase D (PLD)
  • X-ray crystal structure

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free