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| | <StructureSection load='2vpl' size='340' side='right'caption='[[2vpl]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2vpl' size='340' side='right'caption='[[2vpl]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vpl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VPL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vpl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] and [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VPL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zho|1zho]], [[1ad2|1ad2]], [[2j01|2j01]], [[1eg0|1eg0]], [[487d|487d]], [[1u63|1u63]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=2vpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpl OCA], [http://pdbe.org/2vpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vpl RCSB], [http://www.ebi.ac.uk/pdbsum/2vpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpl 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=2vpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpl OCA], [https://pdbe.org/2vpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vpl RCSB], [https://www.ebi.ac.uk/pdbsum/2vpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RL1_THETH RL1_THETH]] The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318] Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318] | + | [https://www.uniprot.org/uniprot/RL1_THETH RL1_THETH] The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318] Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garber, M]] | + | [[Category: Methanocaldococcus jannaschii]] |
| - | [[Category: Kljashtorny, V]] | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Nevskaya, N]] | + | [[Category: Garber M]] |
| - | [[Category: Nikonov, S]] | + | [[Category: Kljashtorny V]] |
| - | [[Category: Tishchenko, S]] | + | [[Category: Nevskaya N]] |
| - | [[Category: Repressor]] | + | [[Category: Nikonov S]] |
| - | [[Category: Ribosomal protein]] | + | [[Category: Tishchenko S]] |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Rna-protein complex]]
| + | |
| - | [[Category: Rrna-binding]]
| + | |
| - | [[Category: Translation]]
| + | |
| - | [[Category: Translation regulation]]
| + | |
| - | [[Category: Trna-binding]]
| + | |
| Structural highlights
Function
RL1_THETH The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318] Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The two-domain ribosomal protein L1 has a dual function as a primary rRNA-binding ribosomal protein and as a translational repressor that binds its own mRNA. Here, we report the crystal structure of a complex between the isolated domain I of L1 from the bacterium Thermus thermophilus and a specific mRNA fragment from Methanoccocus vannielii. In parallel, we report kinetic characteristics measured for complexes formed by intact TthL1 and its domain I with the specific mRNA fragment. Although, there is a close similarity between the RNA-protein contact regions in both complexes, the association rate constant is higher in the case of the complex formed by the isolated domain I. This finding demonstrates that domain II hinders mRNA recognition by the intact TthL1.
Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA.,Tishchenko S, Kljashtorny V, Kostareva O, Nevskaya N, Nikulin A, Gulak P, Piendl W, Garber M, Nikonov S J Mol Biol. 2008 Nov 7;383(2):301-5. Epub 2008 Aug 29. PMID:18778715[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tishchenko S, Kljashtorny V, Kostareva O, Nevskaya N, Nikulin A, Gulak P, Piendl W, Garber M, Nikonov S. Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA. J Mol Biol. 2008 Nov 7;383(2):301-5. Epub 2008 Aug 29. PMID:18778715 doi:10.1016/j.jmb.2008.08.058
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