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Structure of the ribosomal interacting GTPase YjeQ from the enterobacterial species Salmonella typhimurium

Lookup NU author(s): Dr Heather Lamb, Professor Alastair Hawkins


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The YjeQ class of P-loop GTPases assist in ribosome biogenesis and also bind to the 30S subunit of mature ribosomes. YjeQ ribosomal binding is GTP-dependent and thought to specifically direct protein synthesis, although the nature of the upstream signal causing this event in vivo is as yet unknown. The attenuating effect of YjeQ mutants on bacterial growth in Escherichia coli makes it a potential target for novel antimicrobial agents. In order to further explore the structure and function of YjeQ, the isolation, crystallization and structure determination of YjeQ from the enterobacterial species Salmonella typhimurium (StYjeQ) is reported. Whilst the overall StYjeQ fold is similar to those of the previously reported Thematoga maritima and Bacillus subtilis orthologues, particularly the GTPase domain, there are larger differences in the three OB folds. Although the zinc-finger secondary structure is conserved, significant sequence differences alter the nature of the external surface in each case and may reflect varying signalling pathways. Therefore, it may be easier to develop YjeQ-specific inhibitors that target the N- and C-terminal regions, disrupting the metabolic connectivity rather than the GTPase activity. The availability of coordinates for StYjeQ will provide a significantly improved basis for threading Gram-negative orthologue sequences and in silico compound-screening studies, with the potential for the development of species-selective drugs. © International Union of Crystallography 2007.

Publication metadata

Author(s): Nichols CE, Johnson C, Lamb HK, Lockyer M, Charles IG, Hawkins AR, Stammers DK

Publication type: Article

Publication status: Published

Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Year: 2007

Volume: 63

Issue: 11

Pages: 922-928

Print publication date: 01/01/2007

ISSN (print): 1744-3091

ISSN (electronic):

Publisher: Wiley-Blackwell Munksgaard


DOI: 10.1107/S1744309107048609

PubMed id: 18007041


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Funder referenceFunder name
APG19114Biotechnology and Biological Sciences Research Council