View source for 7a05


==NMR structure of D3-D4 domains of Vibrio vulnificus ribosomal protein S1==
<StructureSection load='7a05' size='340' side='right'caption='[[7a05]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7a05]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_vulnificus Vibrio vulnificus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A05 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7a05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a05 OCA], [https://pdbe.org/7a05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a05 RCSB], [https://www.ebi.ac.uk/pdbsum/7a05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a05 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A3Q0L6Y6_VIBVU A0A3Q0L6Y6_VIBVU] Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.[PIRNR:PIRNR002111]
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== Publication Abstract from PubMed ==
The ribosomal S1 protein (rS1) is indispensable for translation initiation in Gram-negative bacteria. rS1 is a multidomain protein that acts as an RNA chaperone and ensures that mRNAs can bind the ribosome in a single-stranded conformation, which could be related to fast recognition. Although many ribosome structures were solved in recent years, a high-resolution structure of a two-domain mRNA-binding competent rS1 construct is not yet available. Here, we present the NMR solution structure of the minimal mRNA-binding fragment of Vibrio Vulnificus rS1 containing the domains D3 and D4. Both domains are homologues and adapt an oligonucleotide-binding fold (OB fold) motif. NMR titration experiments reveal that recognition of miscellaneous mRNAs occurs via a continuous interaction surface to one side of these structurally linked domains. Using a novel paramagnetic relaxation enhancement (PRE) approach and exploring different spin-labeling positions within RNA, we were able to track the location and determine the orientation of the RNA in the rS1-D34 bound form. Our investigations show that paramagnetically labeled RNAs, spiked into unmodified RNA, can be used as a molecular ruler to provide structural information on protein-RNA complexes. The dynamic interaction occurs on a defined binding groove spanning both domains with identical beta2-beta3-beta5 interfaces. Evidently, the 3'-ends of the cis-acting RNAs are positioned in the direction of the N-terminus of the rS1 protein, thus towards the 30S binding site and adopt a conformation required for translation initiation.

NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs.,Qureshi NS, Matzel T, Cetiner EC, Schnieders R, Jonker HRA, Schwalbe H, Furtig B Nucleic Acids Res. 2021 Jul 5. pii: 6315300. doi: 10.1093/nar/gkab562. PMID:34223902<ref>PMID:34223902</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7a05" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribosomal protein S1|Ribosomal protein S1]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio vulnificus]]
[[Category: Cetiner EC]]
[[Category: Fuertig B]]
[[Category: Jonker HRA]]
[[Category: Matzel T]]
[[Category: Qureshi NS]]
[[Category: Schnieders S]]
[[Category: Schwalbe H]]