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5VYP

Crystal structure of the Plant Defensin NsD7 bound to PIP2

Summary for 5VYP
Entry DOI10.2210/pdb5vyp/pdb
DescriptorDefensin NsD7, [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate, SULFATE ION, ... (5 entities in total)
Functional Keywordsantimicrobial, antifungal, defensin, antimicrobial protein
Biological sourceNicotiana suaveolens (Australian tobacco)
Total number of polymer chains24
Total formula weight151086.12
Authors
Jarva, M.,Lay, F.T.,Hulett, M.,Kvansakul, M. (deposition date: 2017-05-25, release date: 2017-08-02, Last modification date: 2023-10-04)
Primary citationJarva, M.,Lay, F.T.,Hulett, M.D.,Kvansakul, M.
Structure of the defensin NsD7 in complex with PIP2 reveals that defensin : lipid oligomer topologies are dependent on lipid type.
FEBS Lett., 591:2482-2490, 2017
Cited by
PubMed Abstract: Defensins are innate immune molecules that upon recognition of specific phospholipids can disrupt microbial membranes by forming oligomeric assemblies. Structures of two related plant defensins, NaD1 and NsD7, bound to phosphatidylinositol 4,5-bisphosphate (PIP ) and phosphatidic acid (PA), respectively, revealed striking differences in their oligomeric topologies. To understand how NsD7 binds different phospholipids and rationalize the different topologies, we determined the structure of an NsD7-PIP complex. This structure reveals fundamental differences in phospholipid binding compared to NsD7-PA, and an oligomeric topology nearly identical to the previously determined NaD1-PIP complex, establishing that the PIP fibril topology is conserved between NaD1 and NsD7. Our findings highlight the remarkable ability of defensins to bind different types of phospholipids to form oligomeric fibrils with diverse topologies.
PubMed: 28741756
DOI: 10.1002/1873-3468.12761
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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