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1t0k

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[[Image:1t0k.gif|left|200px]]
 
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{{Structure
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==Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex==
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|PDB= 1t0k |SIZE=350|CAPTION= <scene name='initialview01'>1t0k</scene>, resolution 3.24&Aring;
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<StructureSection load='1t0k' size='340' side='right'caption='[[1t0k]], [[Resolution|resolution]] 3.24&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=MTT:MALTOTETRAOSE'>MTT</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
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<table><tr><td colspan='2'>[[1t0k]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ck5 1ck5], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ck8 1ck8], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cn8 1cn8] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cn9 1cn9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T0K FirstGlance]. <br>
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|ACTIVITY=
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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]] 3.24&#8491;</td></tr>
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|GENE= MALE, B4034, Z5632, ECS5017 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), RPL30, RPL32, YGL030W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene></td></tr>
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|DOMAIN=
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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=1t0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0k OCA], [https://pdbe.org/1t0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0k RCSB], [https://www.ebi.ac.uk/pdbsum/1t0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0k ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0k OCA], [http://www.ebi.ac.uk/pdbsum/1t0k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t0k RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/RL30_YEAST RL30_YEAST]
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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/t0/1t0k_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=1t0k ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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L30e, a Saccharomyces cervisiae ribosomal protein, regulates its own expression by binding to a purine-rich asymmetric internal loop located in both its pre-mRNA and mature mRNA. A crystal structure of an MBP-L30e fusion protein in complex with an RNA containing the pre-mRNA regulatory site was solved at 3.24 A. Interestingly, the structure of the RNA differed from that observed in a previously determined NMR structure of the complex. Analysis of the NMR data led to the identification of a single imino proton resonance in the internal loop that had been incorrectly assigned and was principally responsible for the erroneous RNA structure. A structure refinement was performed using both the X-ray diffraction data and the NMR-derived distance and angle restraints. The joint NMR and X-ray refinement resulted in improved stereochemistry and lower crystallographic R factors. The RNA internal loop of the MBP-L30e-mRNA complex adopts the canonical K-turn fold.
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'''Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex'''
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Joint X-ray and NMR refinement of the yeast L30e-mRNA complex.,Chao JA, Williamson JR Structure. 2004 Jul;12(7):1165-76. PMID:15242593<ref>PMID:15242593</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1t0k" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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L30e, a Saccharomyces cervisiae ribosomal protein, regulates its own expression by binding to a purine-rich asymmetric internal loop located in both its pre-mRNA and mature mRNA. A crystal structure of an MBP-L30e fusion protein in complex with an RNA containing the pre-mRNA regulatory site was solved at 3.24 A. Interestingly, the structure of the RNA differed from that observed in a previously determined NMR structure of the complex. Analysis of the NMR data led to the identification of a single imino proton resonance in the internal loop that had been incorrectly assigned and was principally responsible for the erroneous RNA structure. A structure refinement was performed using both the X-ray diffraction data and the NMR-derived distance and angle restraints. The joint NMR and X-ray refinement resulted in improved stereochemistry and lower crystallographic R factors. The RNA internal loop of the MBP-L30e-mRNA complex adopts the canonical K-turn fold.
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*[[Kink-turn motif|Kink-turn motif]]
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*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
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==About this Structure==
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*[[Ribosomal protein L30|Ribosomal protein L30]]
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1T0K is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entries 1CK5, 1CK8, 1CN8 and 1CN9. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0K OCA].
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*[[User:Wayne Decatur/kink-turn motif|User:Wayne Decatur/kink-turn motif]]
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== References ==
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==Reference==
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<references/>
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Joint X-ray and NMR refinement of the yeast L30e-mRNA complex., Chao JA, Williamson JR, Structure. 2004 Jul;12(7):1165-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15242593 15242593]
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Chao, J A.]]
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[[Category: Chao JA]]
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[[Category: Williamson, J R.]]
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[[Category: Williamson JR]]
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[[Category: joint nmr and x-ray refinement]]
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[[Category: mbp fusion protein]]
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[[Category: ribosomal protein l30e]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:30 2008''
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Current revision

Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex

PDB ID 1t0k

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