Ergothioneine-biosynthetic sulfoxide synthase EgtB in complex with N,N-dimethyl-histidine and gamma-glutamyl-cysteine

Structure of the Sulfoxide Synthase EgtB from the Ergothioneine Biosynthetic Pathway.

The amino acids GH are left overs from an N-terminal TEV protease cleavage site. The other N- and C-terminal residues are not visible in the electron density and have not been built.

GHMGVAVPHRAELARQLIDARNRTLRLVDFDDAELRRQYDPLMSPLVWDLAHIGQQEELWLLRGGDPRRPGLLEPAVEQL
YDAFVHPRASRVHLPLLSPAQARRFCATVRSAVLDALDRLPEDADTFAFGMVVSHEHQHDETMLQALNLRSGEPLLGSGT
ALPPGRPGVAGTSVLVPGGPFVLGVDLADEPYALDNERPAHVVDVPAFRIGRVPVTNAEWRAFIDDGGYRQRRWWSDAGW
AYRCEAGLTAPQFWNPDGTRTRFGHVEDIPPDEPVQHVTYFEAEAYAAWAGARLPTEIEWEKACAWDPATGRRRRYPWGD
AAPTAALANLGGDALRPAPVGAYPAGASACGAEQMLGDVWEWTSSPLRPWPGFTPMIYQRYSQPFFEGAGSGDYRVLRGG
SWAVAADILRPSFRNWDHPIRRQIFAGVRLAWDVDRQTARPGPVGGC

Mycobacterium thermoresistibile ATCC 19527

0.1 M Tris/HCl pH 7-7.5, 6-12% PEG 8000, 0.2 M magnesium chloride

This entry contains EgtB in its apo form.

This entry contains EgtB in complex with N,N,N-trimethyl-L-histidine.

The biological assembly is a monomer. This was confirmed by size exclusion chromatography. The asymmetric unit contains two biological assemblies

sulfoxide synthase, ergothioneine biosynthesis, C-Lectin, DinB, non-heme Fe(II) enzyme, oxidoreductase

GVAVPHRAELARQLIDARNRTLRLVDFDDAELRRQYDPLMSPLVWDLAHIGQQEELWLLRGGDPRRPGLLEPAVEQLYDA
FVHPRASRVHLPLLSPAQARRFCATVRSAVLDALDRLPEDADTFAFGMVVSHEHQHDETMLQALNLRSGEPLLGSGTALP
PGRPGVAGTSVLVPGGPFVLGVDLADEPYALDNERPAHVVDVPAFRIGRVPVTNAEWRAFIDDGGYRQRRWWSDAGWAYR
CEAGLTAPQFWNPDGTRTRFGHVEDIPPDEPVQHVTYFEAEAYAAWAGARLPTEIEWEKACAWDPATGRRRRYPWGDAAP
TAALANLGGDALRPAPVGAYPAGASACGAEQMLGDVWEWTSSPLRPWPGFTPMIYQRYSQPFFEGAGSGDYRVLRGGSWA
VAADILRPSFRNWDHPIRRQIFAGVRLAWDVDRQTARPGPVGGC