5FF5

Crystal Structure of SeMet PaaA

Summary for 5FF5

• Entry DOI: 10.2210/pdb5ff5/pdb
• Descriptor: PaaA, SULFATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: adenylyltransferase, transferase
• Biological source: Enterobacter agglomerans (Erwinia herbicola, Pantoea agglomerans)
• Total number of polymer chains: 2
• Total formula weight: 87055.27

Authors

Biernat, K.B.,Redinbo, M.R. (deposition date: 2015-12-17, release date: 2016-04-27, Last modification date: 2024-11-20)

Primary citation

Ghodge, S.V.,Biernat, K.A.,Bassett, S.J.,Redinbo, M.R.,Bowers, A.A.
Post-translational Claisen Condensation and Decarboxylation en Route to the Bicyclic Core of Pantocin A.
J.Am.Chem.Soc., 138:5487-5490, 2016

PubMed Abstract: 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.

PubMed: 27088303
DOI: 10.1021/jacs.5b13529

Experimental method

X-RAY DIFFRACTION (2.933 Å)