1EIZ

FTSJ RNA METHYLTRANSFERASE COMPLEXED WITH S-ADENOSYLMETHIONINE

Summary for 1EIZ

• Entry DOI: 10.2210/pdb1eiz/pdb
• Related: 1EJ0
• Descriptor: FTSJ, S-ADENOSYLMETHIONINE (3 entities in total)
• Functional Keywords: ftsj, methyltransferase, adomet, adenosyl methionine, heat shock proteins, 23s ribosomal rna, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 20335.64

Authors

Bugl, H.,Fauman, E.B.,Staker, B.L.,Zheng, F.,Kushner, S.R.,Saper, M.A.,Bardwell, J.C.A.,Jakob, U. (deposition date: 2000-02-29, release date: 2000-08-30, Last modification date: 2024-02-07)

Primary citation

Bugl, H.,Fauman, E.B.,Staker, B.L.,Zheng, F.,Kushner, S.R.,Saper, M.A.,Bardwell, J.C.,Jakob, U.
RNA methylation under heat shock control.
Mol.Cell, 6:349-360, 2000

PubMed Abstract: 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.

PubMed: 10983982
DOI: 10.1016/S1097-2765(00)00035-6

Experimental method

X-RAY DIFFRACTION (1.7 Å)