6mpz | pdb_00006mpz

Crystal structure of a double glycine motif protease from AMS/PCAT transporter in complex with the leader peptide

spinqualitylabelsall models 6mpz, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mpz is a 8 chain structure with sequence from Lachnospiraceae bacterium C6A11 and Prochlorococcus marinus str. MIT 9313. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: 16P, GLZ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The secretion of peptides and proteins is essential for survival and ecological adaptation of bacteria. Dual-functional ATP-binding cassette transporters export antimicrobial or quorum signaling peptides in Gram-positive bacteria. Their substrates contain a leader sequence that is excised by an N-terminal peptidase C39 domain at a double Gly motif. We characterized the protease domain (LahT150) of a transporter from a lanthipeptide biosynthetic operon in Lachnospiraceae and demonstrate that this protease can remove the leader peptide from a diverse set of peptides. The 2.0 A resolution crystal structure of the protease domain in complex with a covalently bound leader peptide demonstrates the basis for substrate recognition across the entire class of such transporters. The structural data also provide a model for understanding the role of leader peptide recognition in the translocation cycle, and the function of degenerate, non-functional C39-like domains (CLD) in substrate recruitment in toxin exporters in Gram-negative bacteria. Insights into AMS/PCAT transporters from biochemical and structural characterization of a double Glycine motif protease.,Bobeica SC, Dong SH, Huo L, Mazo N, McLaughlin MI, Jimenez-Oses G, Nair SK, van der Donk WA Elife. 2019 Jan 14;8. pii: 42305. doi: 10.7554/eLife.42305. PMID:30638446 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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