6fu8: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6fu8' size='340' side='right' caption='[[6fu8]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='6fu8' size='340' side='right' caption='[[6fu8]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fu8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FU8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6fu8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FU8 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=6fu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fu8 OCA], [http://pdbe.org/6fu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fu8 RCSB], [http://www.ebi.ac.uk/pdbsum/6fu8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fu8 ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rplW, Z4689, ECs4183 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=6fu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fu8 OCA], [http://pdbe.org/6fu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fu8 RCSB], [http://www.ebi.ac.uk/pdbsum/6fu8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fu8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 21: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Eco57]] | |||
[[Category: Carroni, M]] | [[Category: Carroni, M]] | ||
[[Category: Heijne, G von]] | [[Category: Heijne, G von]] | ||
Revision as of 11:40, 26 December 2018
uL23 beta hairpin loop deletion of E.coli ribosomeuL23 beta hairpin loop deletion of E.coli ribosome
Structural highlights
Function[RL23_ECO57] 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. Publication Abstract from PubMedThe E.coli ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. Here, using E. coli ribosomes with deletions in loops in proteins uL23 and uL24 that protrude into the tunnel, we investigate how tunnel geometry determines where proteins of different sizes fold. We find that a 29-residue zinc-finger domain normally folding close to the uL23 loop folds deeper in the tunnel in uL23 Dloop ribosomes, while two ~100-residue protein normally folding close to the uL24 loop near the tunnel exit port fold at deeper locations in uL24 Dloop ribosomes, in good agreement with results obtained by coarse-grained molecular dynamics simulations. This supports the idea that cotranslational folding commences once a protein domain reaches a location in the exit tunnel where there is sufficient space to house the folded structure. The shape of the ribosome exit tunnel affects cotranslational protein folding.,Kudva R, Tian P, Pardo-Avila F, Carroni M, Best R, Bernstein HD, von Heijne G Elife. 2018 Nov 26;7. pii: 36326. doi: 10.7554/eLife.36326. PMID:30475203[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||