4nag | pdb_00004nag

Xanthomonins I III are a New Class of Lasso Peptides Featuringa Seven-Membered Macrolactam Ring

spinqualitylabelsall models 4nag, resolution 0.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nag is a 2 chain structure. Full crystallographic information is available from OCA. Ligands: HEZ Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Lasso peptides belong to the class of ribosomally synthesized and post-translationally modified peptides. Their common distinguishing feature is an N-terminal macrolactam ring that is threaded by the C-terminal tail. This lasso fold is maintained through steric interactions. The isolation and characterization of xanthomonins I-III, the first lasso peptides featuring macrolactam rings consisting of only seven amino acids, is now presented. The crystal structure of xanthomonin I and the NMR structure of xanthomonin II were also determined. A total of 25 variants of xanthomonin II were generated to probe different aspects of the biosynthesis, stability, and fold maintenance. These mutational studies reveal the limits such a small ring imposes on the threading and show that every plug amino acid larger than serine is able to maintain a heat-stable lasso fold in the xanthomonin II scaffold. Xanthomonins I-III: A New Class of Lasso Peptides with a Seven-Residue Macrolactam Ring.,Hegemann JD, Zimmermann M, Zhu S, Steuber H, Harms K, Xie X, Marahiel MA Angew Chem Int Ed Engl. 2014 Jan 20. doi: 10.1002/anie.201309267. PMID:24446383 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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