5zyx

Solution NMR structure of K30 peptide in 10 mM dioctanoyl phosphatidylglycerol (D8PG)

spinqualitylabelsall models 5zyx Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zyx is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease A16L1_HUMAN Crohn disease. Disease susceptibility is associated with variations affecting the gene represented in this entry. Function A16L1_HUMAN Plays an essential role in autophagy: interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated form of LC3 named LC3-II. Publication Abstract from PubMed A synthetic antimicrobial peptide library based on the human autophagy 16 polypeptide has been developed. Designed acetylated peptides bearing lipids of different chain lengths, resulted in peptides with enhanced potency compared to the parent Atg16. A 21-residue fragment of Atg16 conjugated to 4-methylhexanoic acid (K30) emerged as the most potent antibacterial, with negligible hemolysis. Several studies, including microscopy, dye leakage and ITC were conducted to gain insight into the antibacterial mechanism of action of the peptide. Visual inspection using both SEM and TEM revealed the membranolytic effect of the peptide on bacterial cells. The selectivity of the peptide against bacterial cell membranes was also proven using dye leakage assays. ITC analysis revealed the exothermic nature of the binding interaction of the peptide to D8PG micelles. Three dimensional solution NMR structure of K30 in complex with dioctanoyl phosphatidylglycerol (D8PG) micelles revealed that the peptide adopts a helix-loop-helix structure in the presence of anionic membrane lipids mimicking bacterial membranes. Intermolecular NOEs between the peptide and lipid deciphered the location of the peptide in the bound state, which was subsequently supported by the paramagnetic relaxation enhancement (PRE) NMR experiment. Collectively, these results describe the structure function relationship of the peptide in the bacterial membrane. Design, Synthesis, Antibacterial Potential and Structural Characterization of N-acylated Derivatives of Human Autophagy 16 Polypeptide.,Varnava KG, Mohid AS, Calligari P, Stella L, Reynisson J, Bhunia A, Sarojini V Bioconjug Chem. 2019 May 30. doi: 10.1021/acs.bioconjchem.9b00290. PMID:31145591 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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