Crystal and solution structures of methyltransferase RsmH provide basis for methylation of C1402 in 16S rRNA

Journal of Structural Biology
Yong WeiYuhui Dong

Abstract

RsmH is a specific AdoMet-dependent methyltransferase (MTase) responsible for N(4)-methylation of C1402 in 16S rRNA and conserved in almost all species of bacteria. The methylcytidine interacts with the P-site codon of the mRNA and increases ribosomal decoding fidelity. In this study, high resolution crystal structure (2.25Å) of Escherichia coli RsmH in complex with AdoMet and cytidine (the putative rRNA binding site) was determined. The structural analysis demonstrated that the complex consists of two distinct but structurally related domains: the typical MTase domain and the putative substrate recognition and binding domain. A deep pocket was found in the conserved AdoMet binding domain. It was also found that the cytidine bound far from AdoMet with the distance of 25.9Å. It indicates that the complex is not in a catalytically active state, and structural rearrangement of RsmH or the nucleotides neighboring C1402 may be necessary to trigger catalysis. Although there is only one molecule in the asymmetric unit of the crystals, RsmH can form a compact dimer across a crystallographic twofold axis. Further analysis of RsmH by small-angle X-ray scattering (SAXS) also revealed the dimer in solution, but with a more flexible conform...Continue Reading

References

Dec 10, 1998·Nucleic Acids Research·J RozenskiJ A McCloskey
Dec 11, 1999·Nucleic Acids Research·R L TatusovE V Koonin
May 24, 2001·Biophysical Journal·D I SvergunM H Koch
Jul 13, 2002·Trends in Biochemical Sciences·Wayne A Decatur, Maurille J Fournier
Dec 2, 2004·Acta Crystallographica. Section D, Biological Crystallography·Paul Emsley, Kevin Cowtan
Apr 7, 2007·Journal of the American Chemical Society·Pau BernadóDmitri I Svergun
Aug 24, 2007·Current Opinion in Structural Biology·Maxim V Petoukhov, Dmitri I Svergun
Sep 27, 2007·ACS Chemical Biology·Christine S ChowSantosh K Mahto
Apr 9, 2008·Nature Structural & Molecular Biology·Zhili XuGloria M Culver
Nov 8, 2008·Molecular Microbiology·Keith ConnollyGloria Culver
Apr 30, 2009·Molecular Microbiology·Elzbieta PurtaStephen Douthwaite
Aug 1, 2007·Journal of Applied Crystallography·Airlie J McCoyRandy J Read

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Citations

Dec 17, 2014·Biochimie·O V SergeevaP V Sergiev
Mar 19, 2014·Biochemical and Biophysical Research Communications·Sun Cheol ParkSung-il Yoon
Mar 25, 2014·Journal of Bacteriology·Jesus M ErasoWilliam Margolin
Sep 10, 2014·Acta Crystallographica. Section F, Structural Biology Communications·Mohan ZhaoJian Wang

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