5NBB

Structure of the C-terminal domain of the Escherichia Coli ProQ RNA binding protein

Summary for 5NBB

• Entry DOI: 10.2210/pdb5nbb/pdb
• NMR Information: BMRB: 34111
• Descriptor: RNA chaperone ProQ (1 entity in total)
• Functional Keywords: fino, proq, rna chaperone, chaperone
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 1
• Total formula weight: 5601.50

Authors

Gonzales, G.,Hardwick, S.,Maslen, S.,Skehel, M.,Holmqvist, E.,Vogel, J.,Bateman, A.,Luisi, B.,Broadhurst, R. (deposition date: 2017-03-01, release date: 2017-05-03, Last modification date: 2024-06-19)

Primary citation

Gonzalez, G.M.,Hardwick, S.W.,Maslen, S.L.,Skehel, J.M.,Holmqvist, E.,Vogel, J.,Bateman, A.,Luisi, B.F.,Broadhurst, R.W.
Structure of the Escherichia coli ProQ RNA-binding protein.
RNA, 23:696-711, 2017

PubMed Abstract: The protein ProQ has recently been identified as a global small noncoding RNA-binding protein in , and a similar role is anticipated for its numerous homologs in divergent bacterial species. We report the solution structure of 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 analysis suggests that the Tudor domain was acquired through horizontal gene transfer and gene fusion to the ancestral FinO-like domain. Through a combination of biochemical and biophysical approaches, we have mapped putative RNA-binding surfaces on all three domains of ProQ and modeled the protein's conformation in the and RNA-bound forms. Taken together, these data suggest how the FinO, Tudor, and linker domains of ProQ cooperate to recognize complex RNA structures and serve to promote RNA-mediated regulation.

PubMed: 28193673
DOI: 10.1261/rna.060343.116

Experimental method

SOLUTION NMR