1zax

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:03, 14 February 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1zax.gif|left|200px]]
 
-
<!--
+
==Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form B==
-
The line below this paragraph, containing "STRUCTURE_1zax", creates the "Structure Box" on the page.
+
<StructureSection load='1zax' size='340' side='right'caption='[[1zax]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1zax]] 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=1ZAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZAX FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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=1zax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zax OCA], [https://pdbe.org/1zax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zax RCSB], [https://www.ebi.ac.uk/pdbsum/1zax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zax ProSAT]</span></td></tr>
-
{{STRUCTURE_1zax| PDB=1zax | SCENE= }}
+
</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/1zax_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=1zax ConSurf].
 +
<div style="clear:both"></div>
-
'''Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form B'''
+
==See Also==
-
 
+
*[[Ribosomal protein L10|Ribosomal protein L10]]
-
 
+
*[[Ribosomal protein L7/L12|Ribosomal protein L7/L12]]
-
==Overview==
+
__TOC__
-
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.
+
</StructureSection>
-
 
+
[[Category: Large Structures]]
-
==About this Structure==
+
-
1ZAX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAX OCA].
+
-
 
+
-
==Reference==
+
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/15989950 15989950]
+
-
[[Category: Protein complex]]
+
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
-
[[Category: Diaconu, M.]]
+
[[Category: Diaconu M]]
-
[[Category: Fischer, N.]]
+
[[Category: Fischer N]]
-
[[Category: Harms, J M.]]
+
[[Category: Harms JM]]
-
[[Category: Kothe, U.]]
+
[[Category: Kothe U]]
-
[[Category: Rodnina, M V.]]
+
[[Category: Rodnina MV]]
-
[[Category: Schluenzen, F.]]
+
[[Category: Schluenzen F]]
-
[[Category: Stark, H.]]
+
[[Category: Stark H]]
-
[[Category: Tonevitski, A G.]]
+
[[Category: Tonevitski AG]]
-
[[Category: Wahl, M C.]]
+
[[Category: Wahl MC]]
-
[[Category: Cryo-electron microscopy]]
+
-
[[Category: Gtpase stimulation]]
+
-
[[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: Thiostrepton loop of 23s rrna]]
+
-
[[Category: Translation factor recruitment]]
+
-
[[Category: X-ray crystallography]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:24:12 2008''
+

Current revision

Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form B

PDB ID 1zax

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools