5dbj | pdb_00005dbj
Crystal structure of halogenase PltA
Structural highlights
FunctionPLTA_PSEF5 Involved in the biosynthesis of the antibiotic pyoluteorin (PubMed:16162666). Catalyzes the dichlorination of the pyrrole ring of pyrrolyl-S-PltL, generating the 5-chloropyrrolyl-S-PltL intermediate and then the 4,5-dichloropyrrolyl-S-PltL product (PubMed:16162666).[1] Publication Abstract from PubMedPyoluteorin is an antifungal agent composed of a 4,5-dichlorinated pyrrole group linked to a resorcinol moiety. The pyoluteorin biosynthetic gene cluster in Pseudomonas fluorescens Pf-5 encodes the halogenase PltA, which has been previously demonstrated to perform both chlorinations in vitro. PltA selectively accepts as a substrate a pyrrole moiety covalently tethered to a nonribosomal peptide thiolation domain PltL (pyrrolyl-S-PltL) for FAD-dependent di-chlorination, yielding 4,5-dichloropyrrolyl-S-PltL. We report a 2.75A-resolution crystal structure of PltA in complex with FAD and chloride. PltA is a dimeric enzyme, containing a flavin-binding fold conserved in flavin-dependent halogenases and monooxygenases, and an additional unique helical region at the C-terminus. This C-terminal region blocks a putative substrate-binding cleft, suggesting that a conformational change involving repositioning of this region is necessary to allow binding of the pyrrolyl-S-PltL substrate for its dichlorination by PltA. Crystal structure of halogenase PltA from the pyoluteorin biosynthetic pathway.,Pang AH, Garneau-Tsodikova S, Tsodikov OV J Struct Biol. 2015 Sep 28. pii: S1047-8477(15)30068-X. doi:, 10.1016/j.jsb.2015.09.013. PMID:26416533[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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