5nbb: Difference between revisions
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The | ==Structure of the N-terminal domain of the Escherichia Coli ProQ RNA binding protein== | ||
<StructureSection load='5nbb' size='340' side='right' caption='[[5nbb]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nbb]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NBB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NBB FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbb OCA], [http://pdbe.org/5nbb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nbb RCSB], [http://www.ebi.ac.uk/pdbsum/5nbb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/PROQ_ECOLI PROQ_ECOLI]] RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism.[HAMAP-Rule:MF_00749]<ref>PMID:21381725</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 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 apo 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. | |||
Structure of the Escherichia coli ProQ RNA-binding protein.,Gonzalez GM, Hardwick SW, Maslen SL, Skehel JM, Holmqvist E, Vogel J, Bateman A, Luisi BF, Broadhurst RW RNA. 2017 May;23(5):696-711. doi: 10.1261/rna.060343.116. Epub 2017 Feb 13. PMID:28193673<ref>PMID:28193673</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5nbb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bateman, A]] | [[Category: Bateman, A]] | ||
[[Category: | [[Category: Broadhurst, R]] | ||
[[Category: Gonzales, G]] | [[Category: Gonzales, G]] | ||
[[Category: Hardwick, S]] | |||
[[Category: Holmqvist, E]] | [[Category: Holmqvist, E]] | ||
[[Category: Luisi, B]] | |||
[[Category: Maslen, S]] | |||
[[Category: Skehel, M]] | [[Category: Skehel, M]] | ||
[[Category: | [[Category: Vogel, J]] | ||
[[Category: | [[Category: Chaperone]] | ||
[[Category: Fino]] | |||
[[Category: Proq]] | |||
[[Category: Rna chaperone]] | |||
