View source for 4beh


==Solution structure of human ribosomal protein P1.P2 heterodimer==
<StructureSection load='4beh' size='340' side='right'caption='[[4beh]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4beh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BEH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=4beh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4beh OCA], [https://pdbe.org/4beh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4beh RCSB], [https://www.ebi.ac.uk/pdbsum/4beh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4beh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RLA1_HUMAN RLA1_HUMAN] Plays an important role in the elongation step of protein synthesis.[HAMAP-Rule:MF_01478]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lateral ribosomal stalk is responsible for binding and recruiting translation factors during protein synthesis. The eukaryotic stalk consists of one P0 protein with two copies of P1*P2 heterodimers to form a P0(P1*P2)2 pentameric P-complex. Here, we have solved the structure of full-length P1*P2 by nuclear magnetic resonance spectroscopy. P1 and P2 dimerize via their helical N-terminal domains, whereas the C-terminal tails of P1*P2 are unstructured and can extend up to approximately 125 A away from the dimerization domains. 15N relaxation study reveals that the C-terminal tails are flexible, having a much faster internal mobility than the N-terminal domains. Replacement of prokaryotic L10(L7/L12)4/L11 by eukaryotic P0(P1*P2)2/eL12 rendered Escherichia coli ribosome, which is insensitive to trichosanthin (TCS), susceptible to depurination by TCS and the C-terminal tail was found to be responsible for this depurination. Truncation and insertion studies showed that depurination of hybrid ribosome is dependent on the length of the proline-alanine rich hinge region within the C-terminal tail. All together, we propose a model that recruitment of TCS to the sarcin-ricin loop required the flexible C-terminal tail, and the proline-alanine rich hinge region lengthens this C-terminal tail, allowing the tail to sweep around the ribosome to recruit TCS.

Solution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome.,Lee KM, Yusa K, Chu LO, Wing-Heng Yu C, Oono M, Miyoshi T, Ito K, Shaw PC, Wong KB, Uchiumi T Nucleic Acids Res. 2013 Jul 26. PMID:23892290<ref>PMID:23892290</ref>

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

==See Also==
*[[Ribosomal protein P1|Ribosomal protein P1]]
*[[Ribosomal protein P2|Ribosomal protein P2]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chu LO]]
[[Category: Ito K]]
[[Category: Lee KM]]
[[Category: Miyoshi T]]
[[Category: Oono M]]
[[Category: Shaw PC]]
[[Category: Uchiumi T]]
[[Category: Wing-Heng Yu C]]
[[Category: Wong KB]]
[[Category: Yusa K]]