|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1zho' size='340' side='right'caption='[[1zho]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1zho' size='340' side='right'caption='[[1zho]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zho]] is a 8 chain structure with sequence from [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=1ZHO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ZHO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zho]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZHO FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1i2a|1i2a]], [[1u63|1u63]], [[1dwu|1dwu]], [[1mzp|1mzp]], [[1ad2|1ad2]], [[1csj|1csj]]</div></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=1zho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zho OCA], [https://pdbe.org/1zho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zho RCSB], [https://www.ebi.ac.uk/pdbsum/1zho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zho ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rplA, rpl1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</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=1zho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zho OCA], [http://pdbe.org/1zho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zho RCSB], [http://www.ebi.ac.uk/pdbsum/1zho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zho 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]] |
| Line 38: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garber, M]] | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Kljashtorny, V]] | + | [[Category: Garber M]] |
| - | [[Category: Kohrer, C]] | + | [[Category: Kljashtorny V]] |
| - | [[Category: Nevskaya, N]] | + | [[Category: Kohrer C]] |
| - | [[Category: Nikonov, O]] | + | [[Category: Nevskaya N]] |
| - | [[Category: Nikonov, S]] | + | [[Category: Nikonov O]] |
| - | [[Category: Nikonova, E]] | + | [[Category: Nikonov S]] |
| - | [[Category: Nikulin, A]] | + | [[Category: Nikonova E]] |
| - | [[Category: Piendl, W]] | + | [[Category: Nikulin A]] |
| - | [[Category: Stockley, P]] | + | [[Category: Piendl W]] |
| - | [[Category: Tishchenko, S]] | + | [[Category: Stockley P]] |
| - | [[Category: Volchkov, S]] | + | [[Category: Tishchenko S]] |
| - | [[Category: Zimmermann, R]] | + | [[Category: Volchkov S]] |
| - | [[Category: L1]]
| + | [[Category: Zimmermann R]] |
| - | [[Category: Mrna-protein complex]]
| + | |
| - | [[Category: Regulation of gene expression]]
| + | |
| - | [[Category: Ribosomal protein]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Rna-protein interaction]]
| + | |
| - | [[Category: Structural protein-rna complex]]
| + | |
| 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 RNA-binding ability of ribosomal protein L1 is of profound interest, since L1 has a dual function as a ribosomal structural protein that binds rRNA and as a translational repressor that binds its own mRNA. Here, we report the crystal structure at 2.6 A resolution of ribosomal protein L1 from the bacterium Thermus thermophilus in complex with a 38 nt fragment of L1 mRNA from Methanoccocus vannielii. The conformation of RNA-bound T.thermophilus L1 differs dramatically from that of the isolated protein. Analysis of four copies of the L1-mRNA complex in the crystal has shown that domain II of the protein does not contribute to mRNA-specific binding. A detailed comparison of the protein-RNA interactions in the L1-mRNA and L1-rRNA complexes identified amino acid residues of L1 crucial for recognition of its specific targets on the both RNAs. Incorporation of the structure of bacterial L1 into a model of the Escherichia coli ribosome revealed two additional contact regions for L1 on the 23S rRNA that were not identified in previous ribosome models.
New insights into the interaction of ribosomal protein L1 with RNA.,Nevskaya N, Tishchenko S, Volchkov S, Kljashtorny V, Nikonova E, Nikonov O, Nikulin A, Kohrer C, Piendl W, Zimmermann R, Stockley P, Garber M, Nikonov S J Mol Biol. 2006 Jan 27;355(4):747-59. Epub 2005 Nov 17. PMID:16330048[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nevskaya N, Tishchenko S, Volchkov S, Kljashtorny V, Nikonova E, Nikonov O, Nikulin A, Kohrer C, Piendl W, Zimmermann R, Stockley P, Garber M, Nikonov S. New insights into the interaction of ribosomal protein L1 with RNA. J Mol Biol. 2006 Jan 27;355(4):747-59. Epub 2005 Nov 17. PMID:16330048 doi:http://dx.doi.org/10.1016/j.jmb.2005.10.084
|
