6o3s | pdb_00006o3s

NMR solution structure of vicilin-buried peptide-8 (VBP-8)

spinqualitylabelsall models 6o3s, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6o3s is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: rRNA N-glycosylase, with EC number 3.2.2.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RIP1_LUFAE] Inhibits protein synthesis in animal cells. Publication Abstract from PubMed New proteins can evolve by duplication and divergence or de novo, from previously non-coding DNA. A recently observed mechanism is for peptides to evolve within a 'host' protein and emerge by proteolytic processing. The first examples of such interstitial peptides were ones hosted by precursors for seed storage albumin. Interstitial peptides have also been observed in precursors for seed vicilins, but current evidence for vicilin-buried peptides (VBPs) is limited to seeds of the broadleaf plants pumpkin and macadamia. Here, an extensive sequence analysis of vicilin precursors suggested that peptides buried within the N-terminal region of preprovicilins are widespread and truly ancient. Gene sequences indicative of interstitial peptides were found in species from Amborellales to eudicots and include important grass and legume crop species. We show the first protein evidence for a monocot VBP in date palm seeds as well as protein evidence from other crops including the common tomato, sesame and pumpkin relatives, cucumber and the sponge loofah (Luffa aegyptiaca). Their excision was consistent with asparaginyl endopeptidase-mediated maturation and sequences were confirmed by tandem mass spectrometry. Our findings suggest the family is large and ancient and, that based on the NMR solution structures for loofah Luffin P1 and tomato VBP-8, VBPs adopt a helical hairpin fold stapled by two internal disulfide bonds. The first VBPs characterized were a protease inhibitor, anti-microbials, and a ribosome inactivator. The age and evolutionary retention of this peptide family suggests its members play important roles in plant biology. An ancient peptide family buried within vicilin precursors.,Zhang J, Payne CD, Pouvreau B, Schaefer H, Fisher MF, Taylor NL, Berkowitz O, Whelan J, Rosengren KJ, Mylne JS ACS Chem Biol. 2019 Apr 11. doi: 10.1021/acschembio.9b00167. PMID:30973714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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