1rqs

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[[Image:1rqs.gif|left|200px]]
 
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==NMR structure of C-terminal domain of ribosomal protein L7 from E.coli==
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The line below this paragraph, containing "STRUCTURE_1rqs", creates the "Structure Box" on the page.
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<StructureSection load='1rqs' size='340' side='right'caption='[[1rqs]]' 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'>[[1rqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7], [https://en.wikipedia.org/wiki/Escherichia_coli_O6 Escherichia coli O6] and [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQS 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">Solution NMR</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=1rqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqs OCA], [https://pdbe.org/1rqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqs RCSB], [https://www.ebi.ac.uk/pdbsum/1rqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqs ProSAT]</span></td></tr>
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{{STRUCTURE_1rqs| PDB=1rqs | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RL7_ECOLI RL7_ECOLI] Seems to be the binding site for several of the factors involved in protein synthesis and appears to be essential for accurate translation.[HAMAP-Rule:MF_00368]
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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/rq/1rqs_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=1rqs 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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Based on the (1)H-(15)N NMR spectroscopy data, the three-dimensional structure and internal dynamic properties of ribosomal protein L7 from Escherichia coli were derived. The structure of L7 dimer in solution can be described as a set of three distinct domains, tumbling rather independently and linked via flexible hinge regions. The dimeric N-terminal domain (residues 1-32) consists of two antiparallel alpha-alpha-hairpins forming a symmetrical four-helical bundle, whereas the two identical C-terminal domains (residues 52-120) adopt a compact alpha/beta-fold. There is an indirect evidence of the existence of transitory helical structures at least in the first part (residues 33-43) of the hinge region. Combining structural data for the ribosomal protein L7/L12 from NMR spectroscopy and x-ray crystallography, it was suggested that its hinge region acts as a molecular switch, initiating "ratchet-like" motions of the L7/L12 stalk with respect to the ribosomal surface in response to elongation factor binding and GTP hydrolysis. This hypothesis allows an explanation of events observed during the translation cycle and provides useful insights into the role of protein L7/L12 in the functioning of the ribosome.
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'''NMR structure of C-terminal domain of ribosomal protein L7 from E.coli'''
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From structure and dynamics of protein L7/L12 to molecular switching in ribosome.,Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT, Arseniev AS J Biol Chem. 2004 Apr 23;279(17):17697-706. Epub 2004 Feb 11. PMID:14960595<ref>PMID:14960595</ref>
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==Overview==
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Based on the (1)H-(15)N NMR spectroscopy data, the three-dimensional structure and internal dynamic properties of ribosomal protein L7 from Escherichia coli were derived. The structure of L7 dimer in solution can be described as a set of three distinct domains, tumbling rather independently and linked via flexible hinge regions. The dimeric N-terminal domain (residues 1-32) consists of two antiparallel alpha-alpha-hairpins forming a symmetrical four-helical bundle, whereas the two identical C-terminal domains (residues 52-120) adopt a compact alpha/beta-fold. There is an indirect evidence of the existence of transitory helical structures at least in the first part (residues 33-43) of the hinge region. Combining structural data for the ribosomal protein L7/L12 from NMR spectroscopy and x-ray crystallography, it was suggested that its hinge region acts as a molecular switch, initiating "ratchet-like" motions of the L7/L12 stalk with respect to the ribosomal surface in response to elongation factor binding and GTP hydrolysis. This hypothesis allows an explanation of events observed during the translation cycle and provides useful insights into the role of protein L7/L12 in the functioning of the ribosome.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1RQS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_escherichia_coli_o6,_escherichia_coli_o157:h7,_and_shigella_flexneri Escherichia coli, escherichia coli o6, escherichia coli o157:h7, and shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQS OCA].
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</div>
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<div class="pdbe-citations 1rqs" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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From structure and dynamics of protein L7/L12 to molecular switching in ribosome., Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT, Arseniev AS, J Biol Chem. 2004 Apr 23;279(17):17697-706. Epub 2004 Feb 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14960595 14960595]
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*[[Ribosomal protein L7/L12|Ribosomal protein L7/L12]]
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[[Category: Escherichia coli, escherichia coli o6, escherichia coli o157:h7, and shigella flexneri]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Arseniev, A S.]]
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__TOC__
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[[Category: Bocharov, E V.]]
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</StructureSection>
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[[Category: Gudkov, A T.]]
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[[Category: Escherichia coli]]
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[[Category: Jaravine, V A.]]
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[[Category: Escherichia coli O157:H7]]
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[[Category: Korzhnev, D M.]]
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[[Category: Escherichia coli O6]]
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[[Category: Pavlov, K V.]]
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[[Category: Large Structures]]
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[[Category: Sobol, A G.]]
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[[Category: Shigella flexneri]]
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[[Category: Nmr]]
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[[Category: Arseniev AS]]
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[[Category: Protein l7/l12,ribosome]]
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[[Category: Bocharov EV]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:48:22 2008''
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[[Category: Gudkov AT]]
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[[Category: Jaravine VA]]
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[[Category: Korzhnev DM]]
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[[Category: Pavlov KV]]
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[[Category: Sobol AG]]

Current revision

NMR structure of C-terminal domain of ribosomal protein L7 from E.coli

PDB ID 1rqs

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