1n88

<StructureSection load='1n88' size='340' side='right'caption='[[1n88]], [[NMR_Ensembles_of_Models | 29 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1n88]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N88 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=1n88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n88 OCA], [https://pdbe.org/1n88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n88 RCSB], [https://www.ebi.ac.uk/pdbsum/1n88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n88 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/RL23_THETH RL23_THETH]] One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome (By similarity).

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== Publication Abstract from PubMed ==

The ribosomal protein L23 is a component of the large ribosomal subunit in which it is located close to the peptide exit tunnel. In this position L23 plays a central role both for protein secretion and folding. We have determined the solution structure of L23 from Thermus thermophilus. Uncomplexed L23 consists of a well-ordered part, with four anti-parallel beta-strands and three alpha-helices connected as beta-alpha-beta-alpha-beta-beta-alpha, and a large and flexible loop inserted between the third and fourth beta-strand. The observed topology is distantly related to previously known structures, primarily within the area of RNA biochemistry. A comparison with RNA-complexed crystal structures of L23 from T. thermophilus, Deinococcus radiodurans and Haloarcula marismourtui, shows that the conformation of the well-ordered part is very similar in the uncomplexed and complexed states. However, the flexible loop found in the uncomplexed solution structure forms a rigid extended structure in the complexed crystal structures as it interacts with rRNA and becomes part of the exit tunnel wall. Structural characteristics of importance for the interaction with rRNA and with the ribosomal protein L29, as well as the functional role of L23, are discussed.

NMR structure of the ribosomal protein L23 from Thermus thermophilus.,Ohman A, Rak A, Dontsova M, Garber MB, Hard T J Biomol NMR. 2003 Jun;26(2):131-7. PMID:12766408<ref>PMID:12766408</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 1n88" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]

[[Category: Dontsova, M]]

[[Category: Garber, M B]]

[[Category: Hard, T]]

[[Category: Ohman, A]]

[[Category: Rak, A]]

[[Category: Translation]]