5DBJ

Crystal structure of halogenase PltA

5DBJ の概要

• エントリーDOI: 10.2210/pdb5dbj/pdb
• 分子名称: FADH2-dependent halogenase PltA, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: halogenase, fad, rossmann fold, pyoluteorin, flavoprotein
• 由来する生物種: Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 261202.14

構造登録者

Pang, A.H.,Tsodikov, O.V. (登録日: 2015-08-21, 公開日: 2015-10-07, 最終更新日: 2023-09-27)

主引用文献

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

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: 26416533
DOI: 10.1016/j.jsb.2015.09.013

実験手法

X-RAY DIFFRACTION (2.75 Å)