7vb2: Difference between revisions
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New page: '''Unreleased structure''' The entry 7vb2 is ON HOLD Authors: Lee, K.M., Wong, K.B. Description: Solution structure of human ribosomal protein uL11 Category: Unreleased Structures ... |
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==Solution structure of human ribosomal protein uL11== | |||
<StructureSection load='7vb2' size='340' side='right'caption='[[7vb2]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7vb2]] is a 1 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=7VB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VB2 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=7vb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vb2 OCA], [https://pdbe.org/7vb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vb2 RCSB], [https://www.ebi.ac.uk/pdbsum/7vb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vb2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RL12_HUMAN RL12_HUMAN] Binds directly to 26S ribosomal RNA (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Eukaryotic uL11 contains a conserved MPPKFDP motif at the N-terminus that is not found in archaeal and bacterial homologs. Here, we determined the solution structure of human uL11 by NMR spectroscopy and characterized its backbone dynamics by 15N-1H relaxation experiments. We showed that these N-terminal residues are unstructured and flexible. Structural comparison with ribosome-bound uL11 suggests that the linker region between the N-terminal domain and C-terminal domain of human uL11 is intrinsically disordered and only becomes structured when bound to the ribosomes. Mutagenesis studies show that the N-terminal conserved MPPKFDP motif is involved in interacting with the P-complex and its extended protuberant domain of uL10 in vitro. Truncation of the MPPKFDP motif also reduced the poly-phenylalanine synthesis in both hybrid ribosome and yeast mutagenesis studies. In addition, G-->A/P substitutions to the conserved GPLG motif of helix-1 reduced poly-phenylalanine synthesis to 9-32% in yeast ribosomes. We propose that the flexible N-terminal residues of uL11, which could extend up to approximately 25 A from the N-terminal domain of uL11, can form transient interactions with the uL10 that help to fetch and fix it into a position ready for recruiting the incoming translation factors and facilitate protein synthesis. | |||
The flexible N-terminal motif of uL11 unique to eukaryotic ribosomes interacts with P-complex and facilitates protein translation.,Yang L, Lee KM, Yu CW, Imai H, Choi AK, Banfield DK, Ito K, Uchiumi T, Wong KB Nucleic Acids Res. 2022 May 20;50(9):5335-5348. doi: 10.1093/nar/gkac292. PMID:35544198<ref>PMID:35544198</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Lee | <div class="pdbe-citations 7vb2" style="background-color:#fffaf0;"></div> | ||
[[Category: Wong | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Lee KM]] | |||
[[Category: Wong KB]] | |||
