FTSJ RNA METHYLTRANSFERASE COMPLEXED WITH S-ADENOSYLMETHIONINE, MERCURY DERIVATIVE

File:1ej0.jpg


1ej0, resolution 1.50Å

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OverviewOverview

Structural, biochemical, and genetic techniques were applied to investigate the function of FtsJ, a recently identified heat shock protein. FtsJ is well conserved, from bacteria to humans. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. The molecular surface of FtsJ exposes a putative nucleic acid binding groove composed of highly conserved, positively charged residues. Substrate analysis showed that FtsJ methylates 23S rRNA within 50S ribosomal subunits in vitro and in vivo. Null mutations in ftsJ show a dramatically altered ribosome profile, a severe growth disadvantage, and a temperature-sensitive phenotype. Our results reveal an unexpected link between the heat shock response and RNA metabolism.

About this StructureAbout this Structure

1EJ0 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

RNA methylation under heat shock control., Bugl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, Jakob U, Mol Cell. 2000 Aug;6(2):349-60. PMID:10983982

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