4q7j

<StructureSection load='4q7j' size='340' side='right'caption='[[4q7j]], [[Resolution|resolution]] 2.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[4q7j]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q7J FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4q7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q7j OCA], [https://pdbe.org/4q7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q7j RCSB], [https://www.ebi.ac.uk/pdbsum/4q7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q7j ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/RS1_ECOLI RS1_ECOLI]] Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. [[https://www.uniprot.org/uniprot/EFTS_ECOLI EFTS_ECOLI]] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.[HAMAP-Rule:MF_00050] [[https://www.uniprot.org/uniprot/EFTU1_ECOLI EFTU1_ECOLI]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]

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== Publication Abstract from PubMed ==

Ribosomal protein S1, consisting of six contiguous OB-folds, is the largest ribosomal protein and is essential for translation initiation in Escherichia coli. S1 is also one of the three essential host-derived subunits of Qbeta replicase, together with EF-Tu and EF-Ts, for Qbeta RNA replication in E. coli. We analyzed the crystal structure of Qbeta replicase, consisting of the virus-encoded RNA-dependent RNA polymerase (beta-subunit), EF-Tu, EF-Ts and the N-terminal half of S1, which is capable of initiating Qbeta RNA replication. Structural and biochemical studies revealed that the two N-terminal OB-folds of S1 anchor S1 onto the beta-subunit, and the third OB-fold is mobile and protrudes beyond the surface of the beta-subunit. The third OB-fold mainly interacts with a specific RNA fragment derived from the internal region of Qbeta RNA, and its RNA-binding ability is required for replication initiation of Qbeta RNA. Thus, the third mobile OB-fold of S1, which is spatially anchored near the surface of the beta-subunit, primarily recruits the Qbeta RNA toward the beta-subunit, leading to the specific and efficient replication initiation of Qbeta RNA, and S1 functions as a replication initiation factor, beyond its established function in protein synthesis.

Molecular insights into replication initiation by Qbeta replicase using ribosomal protein S1.,Takeshita D, Yamashita S, Tomita K Nucleic Acids Res. 2014 Aug 13. pii: gku745. PMID:25122749<ref>PMID:25122749</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 4q7j" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Takeshita, D]]

[[Category: Translation-transferase complex]]