4ht9

From Proteopedia

Crystal structure of E coli Hfq bound to two RNAs

Structural highlights

4ht9 is a 5 chain structure with sequence from Escherichia coli BL21(DE3) and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The rpoS mRNA, which encodes the master regulator sigma(S) of general stress response, requires Hfq-facilitated base pairing with DsrA small RNA for efficient translation at low temperatures. It has recently been proposed that one mechanism underlying Hfq action is to bridge a transient ternary complex by simultaneously binding to rpoS and DsrA. However, no structural evidence of Hfq simultaneously bound to different RNAs has been reported. We detected simultaneous binding of Hfq to rpoS and DsrA fragments. Crystal structures of AU6A*Hfq*A7 and Hfq*A7 complexes were resolved using 1.8- and 1.9-A resolution, respectively. Ternary complex has been further verified in solution by NMR. In vivo, activation of rpoS translation requires intact Hfq, which is capable of bridging rpoS and DsrA simultaneously into ternary complex. This ternary complex possibly corresponds to a meta-stable transition state in Hfq-facilitated small RNA-mRNA annealing process.

Hfq-bridged ternary complex is important for translation activation of rpoS by DsrA.,Wang W, Wang L, Wu J, Gong Q, Shi Y Nucleic Acids Res. 2013 Jun 1;41(11):5938-48. doi: 10.1093/nar/gkt276. Epub 2013 , Apr 19. PMID:23605038^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang W, Wang L, Wu J, Gong Q, Shi Y. Hfq-bridged ternary complex is important for translation activation of rpoS by DsrA. Nucleic Acids Res. 2013 Jun 1;41(11):5938-48. doi: 10.1093/nar/gkt276. Epub 2013 , Apr 19. PMID:23605038 doi:10.1093/nar/gkt276