View source for 1rqt


==NMR structure of dimeric N-terminal domain of ribosomal protein L7 from E.coli==
<StructureSection load='1rqt' size='340' side='right'caption='[[1rqt]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rqt]] 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=1RQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQT FirstGlance]. <br>
</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'>[https://proteopedia.org/fgij/fg.htm?mol=1rqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqt OCA], [https://pdbe.org/1rqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqt RCSB], [https://www.ebi.ac.uk/pdbsum/1rqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqt ProSAT]</span></td></tr>
</table>
== Function ==
[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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== 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<ref>PMID:14960595</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1rqt" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribosomal protein L7/L12|Ribosomal protein L7/L12]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Arseniev AS]]
[[Category: Bocharov EV]]
[[Category: Gudkov AT]]
[[Category: Jaravine VA]]
[[Category: Korzhnev DM]]
[[Category: Pavlov KV]]
[[Category: Sobol AG]]