1zaw
From Proteopedia
(Difference between revisions)
(13 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:1zaw.gif|left|200px]] | ||
- | + | ==Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form A== | |
- | + | <StructureSection load='1zaw' size='340' side='right'caption='[[1zaw]], [[Resolution|resolution]] 2.30Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <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='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='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='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> | |
+ | </table> | ||
+ | == Function == | ||
+ | [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 == | ||
+ | [[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/za/1zaw_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1zaw ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:15989950</ref> | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
+ | <div class="pdbe-citations 1zaw" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Ribosomal protein L10|Ribosomal protein L10]] | |
- | [[Category: | + | *[[Ribosomal protein L7/L12|Ribosomal protein L7/L12]] |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
- | [[Category: Diaconu | + | [[Category: Diaconu M]] |
- | [[Category: Fischer | + | [[Category: Fischer N]] |
- | [[Category: Harms | + | [[Category: Harms JM]] |
- | [[Category: Kothe | + | [[Category: Kothe U]] |
- | [[Category: Rodnina | + | [[Category: Rodnina MV]] |
- | [[Category: Schluenzen | + | [[Category: Schluenzen F]] |
- | [[Category: Stark | + | [[Category: Stark H]] |
- | [[Category: Tonevitski | + | [[Category: Tonevitski AG]] |
- | [[Category: Wahl | + | [[Category: Wahl MC]] |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + |
Current revision
Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form A
|
Categories: Large Structures | Thermotoga maritima | Diaconu M | Fischer N | Harms JM | Kothe U | Rodnina MV | Schluenzen F | Stark H | Tonevitski AG | Wahl MC