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| | <StructureSection load='1dwu' size='340' side='right'caption='[[1dwu]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1dwu' size='340' side='right'caption='[[1dwu]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1dwu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35097 Atcc 35097]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DWU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1DWU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1dwu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DWU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cjs|1cjs]]</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]] 2.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THE CORRESPONDING GENE IN E. COLI IS RPLA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2186 ATCC 35097])</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=1dwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dwu OCA], [https://pdbe.org/1dwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dwu RCSB], [https://www.ebi.ac.uk/pdbsum/1dwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dwu ProSAT]</span></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=1dwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dwu OCA], [http://pdbe.org/1dwu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dwu RCSB], [http://www.ebi.ac.uk/pdbsum/1dwu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dwu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RL1_METTL RL1_METTL]] Probably involved in E site tRNA release (By similarity). Binds directly to 23S rRNA. Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA (By similarity). | + | [https://www.uniprot.org/uniprot/RL1_METTL RL1_METTL] Probably involved in E site tRNA release (By similarity). Binds directly to 23S rRNA. Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA (By similarity). |
| | == 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: Atcc 35097]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garber, M B]] | + | [[Category: Methanothermococcus thermolithotrophicus]] |
| - | [[Category: Nevskaya, N A]] | + | [[Category: Garber MB]] |
| - | [[Category: Nikonov, S V]] | + | [[Category: Nevskaya NA]] |
| - | [[Category: Pavelyev, M N]] | + | [[Category: Nikonov SV]] |
| - | [[Category: Piendl, W]] | + | [[Category: Pavelyev MN]] |
| - | [[Category: Tishchenko, S V]] | + | [[Category: Piendl W]] |
| - | [[Category: Protein synthesis]]
| + | [[Category: Tishchenko SV]] |
| - | [[Category: Ribosomal protein]]
| + | |
| - | [[Category: Rna binding]]
| + | |
| Structural highlights
Function
RL1_METTL Probably involved in E site tRNA release (By similarity). Binds directly to 23S rRNA. Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA (By similarity).
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 crystal structure of ribosomal protein L1 from the archaeon Methanococcus thermolithotrophicus has been determined at 2.7 A resolution. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 67.0, b = 70.1, c = 106.3 A and two molecules per asymmetric unit. The structure was solved by the molecular-replacement method with AMoRe and refined with CNS to an R value of 18.9% and an R(free) of 25.4% in the resolution range 30-2.7 A. Comparison of this structure with those obtained previously for two L1 proteins from other sources (the bacterium Thermus thermophilus and the archaeon M. jannaschii) as well as detailed analysis of intermolecular contacts in the corresponding L1 crystals reveal structural invariants on the molecular surface which are probably important for binding the 23S ribosomal RNA and protein function within the ribosome.
Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface.,Nevskaya N, Tishchenko S, Paveliev M, Smolinskaya Y, Fedorov R, Piendl W, Nakamura Y, Toyoda T, Garber M, Nikonov S Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1023-9. Epub, 2002 May 29. PMID:12037305[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nevskaya N, Tishchenko S, Paveliev M, Smolinskaya Y, Fedorov R, Piendl W, Nakamura Y, Toyoda T, Garber M, Nikonov S. Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface. Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1023-9. Epub, 2002 May 29. PMID:12037305
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