View source for 4toi


==Crystal structure of E.coli ribosomal protein S2 in complex with N-terminal domain of S1==
<StructureSection load='4toi' size='340' side='right'caption='[[4toi]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4toi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_TA206 Escherichia coli TA206]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TOI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4toi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4toi OCA], [https://pdbe.org/4toi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4toi RCSB], [https://www.ebi.ac.uk/pdbsum/4toi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4toi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RS2_ECOLI RS2_ECOLI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In Gram-negative bacteria, the multi-domain protein S1 is essential for translation initiation, as it recruits the mRNA and facilitates its localization in the decoding centre. In sharp contrast to its functional importance, S1 is still lacking from the high-resolution structures available for Escherichia coli and Thermus thermophilus ribosomes and thus the molecular mechanism governing the S1-ribosome interaction has still remained elusive. Here, we present the structure of the N-terminal S1 domain D1 when bound to the ribosome at atomic resolution by using a combination of NMR, X-ray crystallography and cryo-electron microscopy. Together with biochemical assays, the structure reveals that S1 is anchored to the ribosome primarily via a stabilizing pi-stacking interaction within the short but conserved N-terminal segment that is flexibly connected to domain D1. This interaction is further stabilized by salt bridges involving the zinc binding pocket of protein S2. Overall, this work provides one hitherto enigmatic piece in the 'ribosome puzzle', namely the detailed molecular insight into the topology of the S1-ribosome interface. Moreover, our data suggest novel mechanisms that have the potential to modulate protein synthesis in response to environmental cues by changing the affinity of S1 for the ribosome.

Structural basis for the interaction of protein S1 with the Escherichia coli ribosome.,Byrgazov K, Grishkovskaya I, Arenz S, Coudevylle N, Temmel H, Wilson DN, Djinovic-Carugo K, Moll I Nucleic Acids Res. 2014 Dec 15. pii: gku1314. PMID:25510494<ref>PMID:25510494</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4toi" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribosomal protein S1|Ribosomal protein S1]]
*[[Ribosomal protein S2|Ribosomal protein S2]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli TA206]]
[[Category: Large Structures]]
[[Category: Byrgazov K]]
[[Category: Djinovic-Carugo K]]
[[Category: Grishkovskaya I]]
[[Category: Moll I]]