5dm6
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5dm6 is ON HOLD Authors: Kaminishi, T., Schedlbauer, A., Ochoa-Lizarralde, B., Connell, S.R., Fucini, P. Description: Crystal structure of the 50S ...) |
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of the 50S ribosomal subunit from Deinococcus radiodurans== | |
+ | <StructureSection load='5dm6' size='340' side='right'caption='[[5dm6]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5dm6]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DM6 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5dm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dm6 OCA], [https://pdbe.org/5dm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dm6 RCSB], [https://www.ebi.ac.uk/pdbsum/5dm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dm6 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/RL16_DEIRA RL16_DEIRA] Binds the 5S and 23S rRNAs and is also seen to make contacts with the A and P site tRNAs. Interacts with A site tRNA mimics, and is probably one of the key factors, along with a helix of the 23S rRNA, in positioning tRNA stems in the peptidyl-transferase center.[HAMAP-Rule:MF_01342] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Hygromycin A (HygA) binds to the large ribosomal subunit and inhibits its peptidyl transferase (PT) activity. The presented structural and biochemical data indicate that HygA does not interfere with the initial binding of aminoacyl-tRNA to the A site, but prevents its subsequent adjustment such that it fails to act as a substrate in the PT reaction. Structurally we demonstrate that HygA binds within the peptidyl transferase center (PTC) and induces a unique conformation. Specifically in its ribosomal binding site HygA would overlap and clash with aminoacyl-A76 ribose moiety and, therefore, its primary mode of action involves sterically restricting access of the incoming aminoacyl-tRNA to the PTC. | ||
- | + | Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A.,Kaminishi T, Schedlbauer A, Fabbretti A, Brandi L, Ochoa-Lizarralde B, He CG, Milon P, Connell SR, Gualerzi CO, Fucini P Nucleic Acids Res. 2015 Nov 16;43(20):10015-25. doi: 10.1093/nar/gkv975. Epub, 2015 Oct 12. PMID:26464437<ref>PMID:26464437</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: Connell | + | <div class="pdbe-citations 5dm6" style="background-color:#fffaf0;"></div> |
- | [[Category: Fucini | + | == References == |
- | [[Category: Kaminishi | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
+ | [[Category: Deinococcus radiodurans]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Connell SR]] | ||
+ | [[Category: Fucini P]] | ||
+ | [[Category: Kaminishi T]] | ||
+ | [[Category: Ochoa-Lizarralde B]] | ||
+ | [[Category: Schedlbauer A]] |
Current revision
Crystal structure of the 50S ribosomal subunit from Deinococcus radiodurans
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