2k38

Cupiennin 1A, NMR, minimized average structure

spinqualitylabelsall models 2k38 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k38 is a 1 chain structure with sequence from Cupiennius salei. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TXC1A_CUPSA Has antimicrobial activity against B.subtilis, E.coli, E.faecalis, P.denitrificans, P.aeruginosa, P.putida, S.aureus, and S.epidermidis. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane function with its amphipathic structure. Synergistically increases the insecticidal activity of CSTX-1, CSTX-9, and CSTX-13 by up to 65%. Also inhibits the formation of nitric oxide by neuronal nitric oxide synthase. Publication Abstract from PubMed The solution structure of cupiennin 1a, a 35 residue, basic antibacterial peptide isolated from the venom of the spider Cupiennius salei, has been determined by nuclear magnetic resonance (NMR) spectroscopy. The peptide was found to adopt a helix-hinge-helix structure in a membrane mimicking solvent. The hinge may play a role in allowing the amphipathic N-terminal helix and polar C-terminal helix to orient independently upon membrane binding, in order to achieve maximal antibacterial efficacy. Solid-state 31P and 2H NMR was used to further study the effects of cupiennin 1a on the dynamic properties of lipid membranes, using zwitterionic chain deuterated dimyristoylphosphatidylcholine (d54-DMPC) and anionic dimyristoylphosphatidylglycerol (DMPG) multilamellar vesicles. In d54-DMPC alone, cupiennin 1a caused a decrease in the 31P chemical shift anisotropy, indicating some interaction with the lipid head groups, and a decrease in order over the entire acyl chain. In contrast, for the mixed (d54-DMPC/DMPG) lipid system cupiennin 1a appeared to induce lateral separation of the two lipids as evidenced by the 31P spectra, in which the peptide preferentially interacted with DMPG. Little effect was observed on the deuterated acyl chain order parameters in the d54-DMPC/DMPG model membranes. Furthermore, 31P NMR relaxation measurements confirmed a differential effect on the lipid motions depending upon the membrane composition. Therefore, subtle differences are likely in the mechanism by which cupiennin 1a causes membrane lysis in either prokaryotic or eukaryotic cells, and may explain the specific spectrum of activity. Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers.,Pukala TL, Boland MP, Gehman JD, Kuhn-Nentwig L, Separovic F, Bowie JH Biochemistry. 2007 Mar 20;46(11):3576-85. Epub 2007 Feb 24. PMID:17319697 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA