4H6W

Structure of Prenylagaramide maturation protease PagA

Summary for 4H6W

• Entry DOI: 10.2210/pdb4h6w/pdb
• Related: 4h6v 4h6x
• Descriptor: N-terminal cyanobactin protease (2 entities in total)
• Functional Keywords: protease, hydrolase
• Biological source: Planktothrix agardhii NIES-596
• Total number of polymer chains: 2
• Total formula weight: 64176.52

Authors

Nair, S.K.,Agarwal, V. (deposition date: 2012-09-19, release date: 2012-10-03, Last modification date: 2024-10-30)

Primary citation

Agarwal, V.,Pierce, E.,McIntosh, J.,Schmidt, E.W.,Nair, S.K.
Structures of cyanobactin maturation enzymes define a family of transamidating proteases.
Chem.Biol., 19:1411-1422, 2012

PubMed Abstract: Cyanobactins, a class of ribosomally encoded macrocylic natural products, are biosynthesized through the proteolytic processing and subsequent N-C macrocylization of ribosomal peptide precursors. Macrocylization occurs through a two-step process in which the first protease (PatA) removes the amino terminal flanking sequence from the precursor to yield a free N terminus of the precursor peptide, and the second protease (PatG) removes the C-terminal flanking sequence and then catalyzes the transamidation reaction to yield an N-C cyclized product. Here, we present the crystal structures of the protease domains of PatA and PatG from the patellamide cluster and of PagA from the prenylagaramide cluster. A comparative structural and biochemical analysis of the transamidating PatG protease reveals the presence of a unique structural element distinct from canonical subtilisin proteases, which may facilitate the N-C macrocylization of the peptide substrate.

PubMed: 23177196
DOI: 10.1016/j.chembiol.2012.09.012

Experimental method

X-RAY DIFFRACTION (2.45 Å)