2RCN

Crystal Structure of the Ribosomal interacting GTPase YjeQ from the Enterobacterial species Salmonella Typhimurium.

Summary for 2RCN

• Entry DOI: 10.2210/pdb2rcn/pdb
• Descriptor: Probable GTPase engC, ZINC ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: yjeq, gtpase, circularly permuted, gtp-binding, hydrolase, nucleotide-binding
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 1
• Total formula weight: 40428.75

Authors

Nichols, C.E.,Stammers, D.K. (deposition date: 2007-09-20, release date: 2008-01-29, Last modification date: 2023-08-30)

Primary citation

Nichols, C.E.,Johnson, C.,Lamb, H.K.,Lockyer, M.,Charles, I.G.,Hawkins, A.R.,Stammers, D.K.
Structure of the ribosomal interacting GTPase YjeQ from the enterobacterial species Salmonella typhimurium.
Acta Crystallogr.,Sect.F, 63:922-928, 2007

PubMed 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.

PubMed: 18007041
DOI: 10.1107/S1744309107048609

Experimental method

X-RAY DIFFRACTION (2.25 Å)