Phospholipase D

From Proteopedia

spinqualitylabelsall models Phospholipase D complex with substrate dibutyrylphosphatidylcholine (PDB code 1v0y) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Phospholipase D (PLD) hydrolyzes phosphatidylcholine (PC) into phosphatidic acid and choline[1]. PLD is found in organisms ranging from virus to mammals. Relevance Dysregulation of lipid pathways is involved in many neurodegenerative disorders like Alzheimer disease. Brains of Alzheimer disease patients show decreased levels of PC and increased activity of PLD[2]. Structural highlights The [3]. Water molecule are shown as red sphere.

3D structures of phospholipase D

Updated on 05-October-2020

6u8z – hPLD1 catalytic domain 330-500, 643-1074 – human
6ohr – hPLD1 catalytic domain + inhibitor
6ohm, 6oho – hPLD2 catalytic domain 294-933
6ohq, 6ohs, 6ohp – hPLD2 catalytic domain + inhibitor
4rw3 – bsPLD – brown spider
4rw5 – bsPLD (mutant)
3rlg, 3rlh – PLD (mutant) – Loxosceles intemedia
4q6x – PLD – cave spider
2ze4, 1v0r, 1v0s, 1f0i – SaPLD – Streptomyces antibioticus
1v0v, 1v0w – SaPLD + phosphite
1v0y – SaPLD + phosphatidylcholine derivative
2ze9 – SaPLD (mutant) + phosphatidylcholine
1v0t, 1v0u – SaPLD + glycerophosphate
6kz9 – AtPLD a 1 – Arabidopsis thaliana
6kz8 – AtPLD a 1 + phosphatidic acid

References

1. ↑ McDermott M, Wakelam MJ, Morris AJ. Phospholipase D. Biochem Cell Biol. 2004 Feb;82(1):225-53. PMID:15052340 doi:http://dx.doi.org/10.1139/o03-079
2. ↑ Oliveira TG, Di Paolo G. Phospholipase D in brain function and Alzheimer's disease. Biochim Biophys Acta. 2010 Aug;1801(8):799-805. doi:, 10.1016/j.bbalip.2010.04.004. Epub 2010 Apr 23. PMID:20399893 doi:http://dx.doi.org/10.1016/j.bbalip.2010.04.004
3. ↑ Leiros I, McSweeney S, Hough E. The reaction mechanism of phospholipase D from Streptomyces sp. strain PMF. Snapshots along the reaction pathway reveal a pentacoordinate reaction intermediate and an unexpected final product. J Mol Biol. 2004 Jun 11;339(4):805-20. PMID:15165852 doi:http://dx.doi.org/10.1016/j.jmb.2004.04.003