5DBJ
Crystal structure of halogenase PltA
Summary for 5DBJ
| Entry DOI | 10.2210/pdb5dbj/pdb |
| Descriptor | FADH2-dependent halogenase PltA, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | halogenase, fad, rossmann fold, pyoluteorin, flavoprotein |
| Biological source | Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477) |
| Total number of polymer chains | 5 |
| Total formula weight | 261202.14 |
| Authors | Pang, A.H.,Tsodikov, O.V. (deposition date: 2015-08-21, release date: 2015-10-07, Last modification date: 2023-09-27) |
| Primary citation | Pang, A.H.,Garneau-Tsodikova, S.,Tsodikov, O.V. Crystal structure of halogenase PltA from the pyoluteorin biosynthetic pathway. J.Struct.Biol., 192:349-357, 2015 Cited by PubMed Abstract: Pyoluteorin 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 2.75 Å-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. PubMed: 26416533DOI: 10.1016/j.jsb.2015.09.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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