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| | <StructureSection load='1zaw' size='340' side='right'caption='[[1zaw]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1zaw' size='340' side='right'caption='[[1zaw]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zaw]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ZAW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zaw]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZAW FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zav|1zav]], [[1zax|1zax]], [[1zb4|1zb4]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rplJ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589]), rplL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=1zaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zaw OCA], [https://pdbe.org/1zaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zaw RCSB], [https://www.ebi.ac.uk/pdbsum/1zaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zaw ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1zaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zaw OCA], [http://pdbe.org/1zaw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zaw RCSB], [http://www.ebi.ac.uk/pdbsum/1zaw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zaw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RL10_THEMA RL10_THEMA]] Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors (such as IF-2, EF-Tu, EF-G and RF3) (Probable).[HAMAP-Rule:MF_00362] [[http://www.uniprot.org/uniprot/RL7_THEMA RL7_THEMA]] Seems to be the binding site for several of the factors involved in protein synthesis and appears to be essential for accurate translation. | + | [https://www.uniprot.org/uniprot/RL10_THEMA RL10_THEMA] Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors (such as IF-2, EF-Tu, EF-G and RF3) (Probable).[HAMAP-Rule:MF_00362] |
| | == 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: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Diaconu, M]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Fischer, N]] | + | [[Category: Diaconu M]] |
| - | [[Category: Harms, J M]] | + | [[Category: Fischer N]] |
| - | [[Category: Kothe, U]] | + | [[Category: Harms JM]] |
| - | [[Category: Rodnina, M V]] | + | [[Category: Kothe U]] |
| - | [[Category: Schluenzen, F]] | + | [[Category: Rodnina MV]] |
| - | [[Category: Stark, H]] | + | [[Category: Schluenzen F]] |
| - | [[Category: Tonevitski, A G]] | + | [[Category: Stark H]] |
| - | [[Category: Wahl, M C]] | + | [[Category: Tonevitski AG]] |
| - | [[Category: Gtpase stimulation]]
| + | [[Category: Wahl MC]] |
| - | [[Category: L10-l12 complex structure]]
| + | |
| - | [[Category: L10e structure]]
| + | |
| - | [[Category: L7/12 ribosomal stalk]]
| + | |
| - | [[Category: Mechanism of translation]]
| + | |
| - | [[Category: Rapid kinetic]]
| + | |
| - | [[Category: Ribosome structure and function]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Thiostrepton loop of 23s rrna]]
| + | |
| - | [[Category: Translation factor recruitment]]
| + | |
| Structural highlights
Function
RL10_THEMA Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors (such as IF-2, EF-Tu, EF-G and RF3) (Probable).[HAMAP-Rule:MF_00362]
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
The L7/12 stalk of the large subunit of bacterial ribosomes encompasses protein L10 and multiple copies of L7/12. We present crystal structures of Thermotoga maritima L10 in complex with three L7/12 N-terminal-domain dimers, refine the structure of an archaeal L10E N-terminal domain on the 50S subunit, and identify these elements in cryo-electron-microscopic reconstructions of Escherichia coli ribosomes. The mobile C-terminal helix alpha8 of L10 carries three L7/12 dimers in T. maritima and two in E. coli, in concordance with the different length of helix alpha8 of L10 in these organisms. The stalk is organized into three elements (stalk base, L10 helix alpha8-L7/12 N-terminal-domain complex, and L7/12 C-terminal domains) linked by flexible connections. Highly mobile L7/12 C-terminal domains promote recruitment of translation factors to the ribosome and stimulate GTP hydrolysis by the ribosome bound factors through stabilization of their active GTPase conformation.
Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation.,Diaconu M, Kothe U, Schlunzen F, Fischer N, Harms JM, Tonevitsky AG, Stark H, Rodnina MV, Wahl MC Cell. 2005 Jul 1;121(7):991-1004. PMID:15989950[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Diaconu M, Kothe U, Schlunzen F, Fischer N, Harms JM, Tonevitsky AG, Stark H, Rodnina MV, Wahl MC. Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation. Cell. 2005 Jul 1;121(7):991-1004. PMID:15989950 doi:10.1016/j.cell.2005.04.015
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