4v4p: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v4p]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yl3 1yl3] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yl4 1yl4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4P FirstGlance]. <br> | <table><tr><td colspan='2'>[[4v4p]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yl3 1yl3] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yl4 1yl4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4P 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=4v4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4p OCA], [https://pdbe.org/4v4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4p RCSB], [https://www.ebi.ac.uk/pdbsum/4v4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4p ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 5.5Å</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=4v4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4p OCA], [https://pdbe.org/4v4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4p RCSB], [https://www.ebi.ac.uk/pdbsum/4v4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4p ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == |
Latest revision as of 21:03, 20 September 2023
Crystal structure of 70S ribosome with thrS operator and tRNAs.Crystal structure of 70S ribosome with thrS operator and tRNAs.
Structural highlights
FunctionRS16_THET8 Binds to the lower part of the body of the 30S subunit, where it stabilizes two of its domains.[HAMAP-Rule:MF_00385] Publication Abstract from PubMedThe ribosome of Thermus thermophilus was cocrystallized with initiator transfer RNA (tRNA) and a structured messenger RNA (mRNA) carrying a translational operator. The path of the mRNA was defined at 5.5 angstroms resolution by comparing it with either the crystal structure of the same ribosomal complex lacking mRNA or with an unstructured mRNA. A precise ribosomal environment positions the operator stem-loop structure perpendicular to the surface of the ribosome on the platform of the 30S subunit. The binding of the operator and of the initiator tRNA occurs on the ribosome with an unoccupied tRNA exit site, which is expected for an initiation complex. The positioning of the regulatory domain of the operator relative to the ribosome elucidates the molecular mechanism by which the bound repressor switches off translation. Our data suggest a general way in which mRNA control elements must be placed on the ribosome to perform their regulatory task. Translational operator of mRNA on the ribosome: how repressor proteins exclude ribosome binding.,Jenner L, Romby P, Rees B, Schulze-Briese C, Springer M, Ehresmann C, Ehresmann B, Moras D, Yusupova G, Yusupov M Science. 2005 Apr 1;308(5718):120-3. PMID:15802605[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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