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

Nichols, CE; Johnson, C; Lamb, HK; Lockyer, M; Charles, IG; Hawkins, AR; Stammers, DK

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

Nichols, CE Johnson, C Lamb, HK Lockyer, M Charles, IG Hawkins, AR Stammers, DK

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Publisher:: Blackwell Publishing
Publication Type:: Journal Article
Citation:: Acta Crystallographica Section F-Structural Biology And Crystallization Communications, 2007, 63 (11), pp. 922 - 928
Issue Date:: 2007-01

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Field	Value	Language
dc.contributor.author	Nichols, CE	en_US
dc.contributor.author	Johnson, C	en_US
dc.contributor.author	Lamb, HK	en_US
dc.contributor.author	Lockyer, M	en_US
dc.contributor.author	Charles, IG	en_US
dc.contributor.author	Hawkins, AR	en_US
dc.contributor.author	Stammers, DK	en_US
dc.date.issued	2007-01	en_US
dc.identifier.citation	Acta Crystallographica Section F-Structural Biology And Crystallization Communications, 2007, 63 (11), pp. 922 - 928	en_US
dc.identifier.issn	1744-3091	en_US
dc.identifier.uri	http://hdl.handle.net/10453/13350
dc.description.abstract	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.	en_US
dc.publisher	Blackwell Publishing	en_US
dc.relation.ispartof	Acta Crystallographica Section F-Structural Biology And Crystallization Communications	en_US
dc.relation.isbasedon	10.1107/S1744309107048609	en_US
dc.subject.classification	Biophysics	en_US
dc.title	Structure of the ribosomal interacting GTPase YjeQ from the enterobacterial species Salmonella typhimurium	en_US
dc.type	Journal Article
utslib.citation.volume	11	en_US
utslib.citation.volume	63	en_US
utslib.for	0304 Medicinal and Biomolecular Chemistry	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	06 Biological Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access
pubs.consider-herdc	false	en_US
pubs.issue	11	en_US
pubs.volume	63	en_US

Abstract:

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.

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http://hdl.handle.net/10453/13350