1rqu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1rqu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rqu" /> '''NMR structure of L7 dimer from E.coli'''<br ...)
Current revision (09:06, 22 May 2024) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1rqu.gif|left|200px]]<br /><applet load="1rqu" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1rqu" />
 
-
'''NMR structure of L7 dimer from E.coli'''<br />
 
-
==Overview==
+
==NMR structure of L7 dimer from E.coli==
-
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.
+
<StructureSection load='1rqu' size='340' side='right'caption='[[1rqu]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1rqu]] 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=1RQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQU 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=1rqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqu OCA], [https://pdbe.org/1rqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqu RCSB], [https://www.ebi.ac.uk/pdbsum/1rqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqu 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]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rq/1rqu_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1rqu ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
==About this Structure==
+
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>
-
1RQU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RQU OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14960595 14960595]
+
</div>
-
[[Category: Escherichia coli]]
+
<div class="pdbe-citations 1rqu" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Arseniev, A.S.]]
+
-
[[Category: Bocharov, E.V.]]
+
-
[[Category: Gudkov, A.T.]]
+
-
[[Category: Jaravine, V.A.]]
+
-
[[Category: Korzhnev, D.M.]]
+
-
[[Category: Pavlov, K.V.]]
+
-
[[Category: Sobol, A.G.]]
+
-
[[Category: nmr]]
+
-
[[Category: protein l7/l12]]
+
-
[[Category: ribosome]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:48:25 2007''
+
==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]]

Current revision

NMR structure of L7 dimer from E.coli

PDB ID 1rqu

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools