2oum

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[[Image:2oum.jpg|left|200px]]
 
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==The first domain of L1 from Thermus thermophilus==
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The line below this paragraph, containing "STRUCTURE_2oum", creates the "Structure Box" on the page.
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<StructureSection load='2oum' size='340' side='right'caption='[[2oum]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2oum]] is a 1 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=2OUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OUM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oum OCA], [https://pdbe.org/2oum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oum RCSB], [https://www.ebi.ac.uk/pdbsum/2oum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oum ProSAT]</span></td></tr>
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{{STRUCTURE_2oum| PDB=2oum | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RL1_THET8 RL1_THET8] Directly binds to 23S rRNA. Forms what is known as the L1 stalk, which protrudes beyond the 70S ribosome surface. The stalk is preferentially stabilized in 70S versus 50S crystals. Interacts with the E site tRNA, blocking the exit path. This blockage implies that this section of the ribosome must be able to move to release the deacetylated tRNA.[HAMAP-Rule:MF_01318_B] 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_B]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/2oum_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2oum ConSurf].
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<div style="clear:both"></div>
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'''The first domain of L1 from Thermus thermophilus'''
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==See Also==
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*[[Ribosomal protein L1|Ribosomal protein L1]]
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__TOC__
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==Overview==
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</StructureSection>
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Ribosomal protein L1 has a dual function as a ribosomal protein binding 23S rRNA and as a translational repressor binding its mRNA. L1 is a two-domain protein with N- and C-termini located in domain I. Earlier it was shown that L1 interacts with the same targets on both rRNA and mRNA mainly through domain I. We have suggested that domain I is necessary and sufficient for specific RNA-binding by L1. To test this hypothesis, a truncation mutant of L1 from Thermus thermophilus, representing domain I, was constructed by deletion of the central part of the L1 sequence, which corresponds to domain II. It was shown that the isolated domain I forms stable complexes with specific fragments of both rRNA and mRNA. The crystal structure of the isolated domain I was determined and compared with the structure of this domain within the intact protein L1. This comparison revealed a close similarity of both structures. Our results confirm our suggestion that in protein L1 its domain I alone is sufficient for specific RNA binding, whereas domain II stabilizes the L1-rRNA complex.
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[[Category: Large Structures]]
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==About this Structure==
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2OUM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUM OCA].
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==Reference==
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Domain I of ribosomal protein L1 is sufficient for specific RNA binding., Tishchenko S, Nikonova E, Kljashtorny V, Kostareva O, Nevskaya N, Piendl W, Davydova N, Streltsov V, Garber M, Nikonov S, Nucleic Acids Res. 2007;35(21):7389-95. Epub 2007 Oct 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17962298 17962298]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
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[[Category: Davydova, N.]]
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[[Category: Garber, M.]]
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[[Category: Kljashtorny, V.]]
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[[Category: Nevskaya, N.]]
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[[Category: Nikonov, S.]]
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[[Category: Tishchenko, S.]]
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[[Category: Ribosomal protein l1]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:41:26 2008''
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[[Category: Davydova N]]
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[[Category: Garber M]]
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[[Category: Kljashtorny V]]
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[[Category: Nevskaya N]]
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[[Category: Nikonov S]]
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[[Category: Tishchenko S]]

Current revision

The first domain of L1 from Thermus thermophilus

PDB ID 2oum

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