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| <StructureSection load='1njn' size='340' side='right'caption='[[1njn]], [[Resolution|resolution]] 3.70Å' scene=''> | | <StructureSection load='1njn' size='340' side='right'caption='[[1njn]], [[Resolution|resolution]] 3.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1njn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NJN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1njn]] is a 1 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=1NJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NJN FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SPS:SPARSOMYCIN'>SPS</scene></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]] 3.7Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1njm|1njm]], [[1njo|1njo]], [[1njp|1njp]], [[1k01|1k01]], [[1jzx|1jzx]], [[1jzy|1jzy]], [[1jzz|1jzz]], [[1k00|1k00]], [[1nkw|1nkw]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SPS:SPARSOMYCIN'>SPS</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1njn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1njn OCA], [http://pdbe.org/1njn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1njn RCSB], [http://www.ebi.ac.uk/pdbsum/1njn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1njn ProSAT]</span></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=1njn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1njn OCA], [https://pdbe.org/1njn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1njn RCSB], [https://www.ebi.ac.uk/pdbsum/1njn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1njn ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| [[Category: Deinococcus radiodurans]] | | [[Category: Deinococcus radiodurans]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Agmon, I]] | + | [[Category: Agmon I]] |
- | [[Category: Bartels, H]] | + | [[Category: Bartels H]] |
- | [[Category: Bashan, A]] | + | [[Category: Bashan A]] |
- | [[Category: Berisio, R]] | + | [[Category: Berisio R]] |
- | [[Category: Hansen, H A]] | + | [[Category: Hansen HA]] |
- | [[Category: Harms, J M]] | + | [[Category: Harms JM]] |
- | [[Category: Schluenzen, F]] | + | [[Category: Schluenzen F]] |
- | [[Category: Yonath, A]] | + | [[Category: Yonath A]] |
- | [[Category: Zarivatch, R]] | + | [[Category: Zarivatch R]] |
- | [[Category: Peptide bond formation]]
| + | |
- | [[Category: Peptidyl-transferase]]
| + | |
- | [[Category: Puromycin]]
| + | |
- | [[Category: Ribosome]]
| + | |
- | [[Category: Sparsomycin]]
| + | |
- | [[Category: Trna]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3' end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.
Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression.,Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J, Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen HA, Kossoy E, Kessler M, Yonath A Mol Cell. 2003 Jan;11(1):91-102. PMID:12535524[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J, Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen HA, Kossoy E, Kessler M, Yonath A. Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression. Mol Cell. 2003 Jan;11(1):91-102. PMID:12535524
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