4urd: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4urd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4URD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4URD FirstGlance]. <br> | <table><tr><td colspan='2'>[[4urd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4URD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4URD FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4urd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4urd OCA], [http://pdbe.org/4urd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4urd RCSB], [http://www.ebi.ac.uk/pdbsum/4urd PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4urd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4urd OCA], [http://pdbe.org/4urd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4urd RCSB], [http://www.ebi.ac.uk/pdbsum/4urd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4urd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
Trigger factor (TF) is the only ribosome-associated chaperone in bacteria. It interacts with hydrophobic segments in nascent chain (NCs) as they emerge from the ribosome. TF binds via its N-terminal ribosome-binding domain (RBD) mainly to ribosomal protein uL23 at the tunnel exit on the large ribosomal subunit. Whereas earlier structural data suggested that TF binds as a rigid molecule to the ribosome, recent comparisons of structural data on substrate-bound, ribosome-bound, and TF in solution from different species suggest that this chaperone is a rather flexible molecule. Here, we present two cryo-electron microscopy structures of TF bound to ribosomes translating an mRNA coding for a known TF substrate from Escherichia coli of a different length. The structures reveal distinct degrees of flexibility for the different TF domains, a conformational rearrangement of the RBD upon ribosome binding, and an increase in rigidity within TF when the NC is extended. Molecular dynamics simulations agree with these data and offer a molecular basis for these observations. | |||
Dynamic Behavior of Trigger Factor on the Ribosome.,Deeng J, Chan KY, van der Sluis EO, Berninghausen O, Han W, Gumbart J, Schulten K, Beatrix B, Beckmann R J Mol Biol. 2016 Jun 16. pii: S0022-2836(16)30215-7. doi:, 10.1016/j.jmb.2016.06.007. PMID:27320387<ref>PMID:27320387</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 4urd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
