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| | ==Spatial model of L7 dimer from E.coli with one hinge region in helical state== | | ==Spatial model of L7 dimer from E.coli with one hinge region in helical state== |
| - | <StructureSection load='1rqv' size='340' side='right'caption='[[1rqv]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1rqv' size='340' side='right'caption='[[1rqv]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rqv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RQV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rqv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQV FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rqs|1rqs]], [[1rqt|1rqt]], [[1rqu|1rqu]], [[1dd3|1dd3]], [[1dd4|1dd4]], [[1ctf|1ctf]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqv OCA], [http://pdbe.org/1rqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rqv RCSB], [http://www.ebi.ac.uk/pdbsum/1rqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqv ProSAT]</span></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=1rqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqv OCA], [https://pdbe.org/1rqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqv RCSB], [https://www.ebi.ac.uk/pdbsum/1rqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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] | + | [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] |
| | == 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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arseniev, A S]] | + | [[Category: Arseniev AS]] |
| - | [[Category: Bocharov, E V]] | + | [[Category: Bocharov EV]] |
| - | [[Category: Gudkov, A T]] | + | [[Category: Gudkov AT]] |
| - | [[Category: Jaravine, V A]] | + | [[Category: Jaravine VA]] |
| - | [[Category: Korzhnev, D M]] | + | [[Category: Korzhnev DM]] |
| - | [[Category: Pavlov, K V]] | + | [[Category: Pavlov KV]] |
| - | [[Category: Sobol, A G]] | + | [[Category: Sobol AG]] |
| - | [[Category: Protein l7/l12]]
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| - | [[Category: Ribosome]]
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| Structural highlights
Function
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]
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
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT, Arseniev AS. From structure and dynamics of protein L7/L12 to molecular switching in ribosome. J Biol Chem. 2004 Apr 23;279(17):17697-706. Epub 2004 Feb 11. PMID:14960595 doi:10.1074/jbc.M313384200
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