2017
DOI: 10.1261/rna.060343.116
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Structure of the Escherichia coli ProQ RNA-binding protein

Abstract: The protein ProQ has recently been identified as a global small noncoding RNA-binding protein in Salmonella, and a similar role is anticipated for its numerous homologs in divergent bacterial species. We report the solution structure of Escherichia coli ProQ, revealing an N-terminal FinO-like domain, a C-terminal domain that unexpectedly has a Tudor domain fold commonly found in eukaryotes, and an elongated bridging intradomain linker that is flexible but nonetheless incompressible. Structure-based sequence an… Show more

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Cited by 51 publications
(121 citation statements)
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References 40 publications
(52 reference statements)
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“…For E. coli ProQ, the structure of the N-terminal 121amino acid FinO-like domain was initially modeled based on that of FinO (Smith et al, 2004(Smith et al, , 2007. A recent NMR solution structure of the isolated N-terminal domain (residues 1-119) confirmed that its fold is similar to that of the central domain of FinO, again with multiple positively charged residues on the concave surface (Gonzalez et al, 2017). However, the convex side is more highly charged with distinct positive and negative patches (Fig.…”
Section: Structures Of Fino-domain Proteinsmentioning
confidence: 99%
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“…For E. coli ProQ, the structure of the N-terminal 121amino acid FinO-like domain was initially modeled based on that of FinO (Smith et al, 2004(Smith et al, , 2007. A recent NMR solution structure of the isolated N-terminal domain (residues 1-119) confirmed that its fold is similar to that of the central domain of FinO, again with multiple positively charged residues on the concave surface (Gonzalez et al, 2017). However, the convex side is more highly charged with distinct positive and negative patches (Fig.…”
Section: Structures Of Fino-domain Proteinsmentioning
confidence: 99%
“…Later it was compared with the Sm-like domain, and hence was termed Hfq-like, despite little sequence homology and the lack of the a-helix motif characteristic of Sm folds (Smith et al, 2007). Most recently, the NMR structure determined for the isolated C-terminal domain (residues 180-232) shows the tertiary structure is most similar to Tudor domains, which promote binding to proteins with modified amino acids (Gonzalez et al, 2017). Overall the surface of this domain is mostly electrostatically neutral.…”
Section: Many Fino-domain Proteins Have N-or C-terminal Extensionsmentioning
confidence: 99%
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