5ff5

Crystal Structure of SeMet PaaA

spinqualitylabelsall models 5ff5, resolution 2.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ff5 is a 2 chain structure with sequence from Pantoea agglomerans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.933Å Ligands: GOL, MSE, NI, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9ZAR3_ENTAG Publication Abstract from PubMed Pantocin A (PA) is a member of the growing family of ribosomally encoded and post-translationally modified peptide natural products (RiPPs). PA is much smaller than most known RiPPs, a tripeptide with a tight bicyclic core that appears to be cleaved from the middle of a larger 30-residue precursor peptide. We show here that the enzyme PaaA catalyzes the double dehydration and decarboxylation of two glutamic acid residues in the 30-residue precursor PaaP. Further truncates of PaaP leader and follower peptide sequences demonstrate the different impacts of these two regions on PaaA-mediated tailoring and delineate an essential role for the follower sequence in the decarboxylation step. The crystal structure of apo PaaA is reported, allowing identification of structural features that set PaaA apart from other homologous enzymes that typically do not catalyze such extended post-translational chemistry. Together, these data reveal how additional chemistry can be extracted from a ubiquitous enzyme family toward ribosomally derived peptide natural product biosynthesis and suggest that more examples of such enzymes likely exist in untapped genomic space. Post-translational Claisen Condensation and Decarboxylation en Route to the Bicyclic Core of Pantocin A.,Ghodge SV, Biernat KA, Bassett SJ, Redinbo MR, Bowers AA J Am Chem Soc. 2016 May 4;138(17):5487-90. doi: 10.1021/jacs.5b13529. Epub 2016, Apr 22. PMID:27088303 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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