4zu9: Difference between revisions

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'''Unreleased structure'''


The entry 4zu9 is ON HOLD  until Paper Publication
==Crystal structure of bacterial selenocysteine-specific elongation factor EF-Sec==
<StructureSection load='4zu9' size='340' side='right'caption='[[4zu9]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zu9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZU9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4zu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zu9 OCA], [https://pdbe.org/4zu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zu9 RCSB], [https://www.ebi.ac.uk/pdbsum/4zu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zu9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O67141_AQUAE O67141_AQUAE]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Selenocysteine (Sec), the 21(st) amino acid in translation, uses its specific tRNA (tRNA(Sec)) to recognize the UGA codon. The Sec-specific elongation factor SelB brings the selenocysteinyl-tRNA(Sec) (Sec-tRNA(Sec)) to the ribosome, dependent on both an in-frame UGA and a Sec-insertion sequence (SECIS) in the mRNA. The bacterial SelB binds mRNA through its C-terminal region, for which crystal structures have been reported. In this study, we determined the crystal structure of the full-length SelB from the bacterium Aquifex aeolicus, in complex with a GTP analog, at 3.2-A resolution. SelB consists of three EF-Tu-like domains (D1-3), followed by four winged-helix domains (WHD1-4). The spacer region, connecting the N- and C-terminal halves, fixes the position of WHD1 relative to D3. The binding site for the Sec moiety of Sec-tRNA(Sec) is located on the interface between D1 and D2, where a cysteine molecule from the crystallization solution is coordinated by Arg residues, which may mimic Sec binding. The Sec-binding site is smaller and more exposed than the corresponding site of EF-Tu. Complex models of Sec-tRNA(Sec), SECIS RNA, and the 70S ribosome suggest that the unique secondary structure of tRNA(Sec) allows SelB to specifically recognize tRNA(Sec) and characteristically place it at the ribosomal A-site.


Authors: Itoh, Y., Sekine, S., Yokoyama, S.
Crystal structure of the full-length bacterial selenocysteine-specific elongation factor SelB.,Itoh Y, Sekine S, Yokoyama S Nucleic Acids Res. 2015 Oct 15;43(18):9028-38. doi: 10.1093/nar/gkv833. Epub 2015, Aug 24. PMID:26304550<ref>PMID:26304550</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Sekine, S]]
<div class="pdbe-citations 4zu9" style="background-color:#fffaf0;"></div>
[[Category: Yokoyama, S]]
 
[[Category: Itoh, Y]]
==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus VF5]]
[[Category: Large Structures]]
[[Category: Itoh Y]]
[[Category: Sekine S]]
[[Category: Yokoyama S]]

Latest revision as of 07:42, 18 May 2023

Crystal structure of bacterial selenocysteine-specific elongation factor EF-Sec

4zu9, resolution 3.19Å

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