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| | <StructureSection load='4q7j' size='340' side='right'caption='[[4q7j]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='4q7j' size='340' side='right'caption='[[4q7j]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4q7j]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Allolevivirus_subgroup_iii Allolevivirus subgroup iii] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q7J FirstGlance]. <br> | + | <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"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3agp|3agp]], [[3agq|3agq]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3agp|3agp]], [[3agq|3agq]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tsf ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), tufA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), rpsA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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> |
| - | <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=4q7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q7j OCA], [http://pdbe.org/4q7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q7j RCSB], [http://www.ebi.ac.uk/pdbsum/4q7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q7j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. [[http://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] [[http://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] | + | [[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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Elongation factor|Elongation factor]] | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| | *[[Ribosomal protein S1|Ribosomal protein S1]] | | *[[Ribosomal protein S1|Ribosomal protein S1]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Allolevivirus subgroup iii]] | |
| - | [[Category: Ecoli]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Takeshita, D]] | | [[Category: Takeshita, D]] |
| Structural highlights
Function
[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. [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] [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]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Takeshita D, Yamashita S, Tomita K. Molecular insights into replication initiation by Qbeta replicase using ribosomal protein S1. Nucleic Acids Res. 2014 Aug 13. pii: gku745. PMID:25122749 doi:http://dx.doi.org/10.1093/nar/gku745
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