1gyz

<StructureSection load='1gyz' size='340' side='right'caption='[[1gyz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1gyz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquae Aquae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYZ 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=1gyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyz OCA], [https://pdbe.org/1gyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gyz RCSB], [https://www.ebi.ac.uk/pdbsum/1gyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gyz ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/RL20_AQUAE RL20_AQUAE]] Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity).

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== Publication Abstract from PubMed ==

L20 is a specific protein of the bacterial ribosome, which is involved in the early assembly steps of the 50S subunit and in the feedback control of the expression of its own gene. This dual function involves specific interactions with either the 23S rRNA or its messenger RNA. The solution structure of the free Aquifex aeolicus L20 has been solved. It is composed of an unstructured N-terminal domain comprising residues 1-58 and a C-terminal alpha-helical domain. This is in contrast with what is observed in the bacterial 50S subunit, where the N-terminal region folds as an elongated alpha-helical region. The solution structure of the C-terminal domain shows that several solvent-accessible, conserved residues are clustered on the surface of the molecule and are probably involved in RNA recognition. In vivo studies show that this domain is sufficient to repress the expression of the cistrons encoding L35 and L20 in the IF3 operon. The ability of L20 C-terminal domain to specifically recognise RNA suggests an assembly mechanism for L20 into the ribosome. The pre-folded C-terminal domain would make a primary interaction with a specific site on the 23S rRNA. The N-terminal domain would then fold within the ribosome, participating in its correct 3D assembly.

NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.,Raibaud S, Lebars I, Guillier M, Chiaruttini C, Bontems F, Rak A, Garber M, Allemand F, Springer M, Dardel F J Mol Biol. 2002 Oct 11;323(1):143-51. PMID:12368106<ref>PMID:12368106</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 1gyz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Aquae]]

[[Category: Bontems, F]]

[[Category: Dardel, F]]

[[Category: Lebars, I]]

[[Category: Raibaud, S]]

[[Category: Translational control]]