1zax: Difference between revisions

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[[Image:1zax.png|left|200px]]
==Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form B==
<StructureSection load='1zax' size='340' side='right' caption='[[1zax]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zax]] is a 7 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZAX FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zav|1zav]], [[1zaw|1zaw]]</td></tr>
<tr><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 Thermotoga maritima]), rplL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zax OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zax RCSB], [http://www.ebi.ac.uk/pdbsum/1zax PDBsum]</span></td></tr>
<table>
== 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/chain_selection.php?pdb_ID=2ata 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.


{{STRUCTURE_1zax|  PDB=1zax  |  SCENE=  }}
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>


===Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form B===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_15989950}}
 
==About this Structure==
[[1zax]] is a 7 chain structure with sequence 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].


==See Also==
==See Also==
*[[Ribosomal protein L10|Ribosomal protein L10]]
*[[Ribosomal protein L10|Ribosomal protein L10]]
*[[Ribosomal protein L7|Ribosomal protein L7]]
*[[Ribosomal protein L7|Ribosomal protein L7]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:015989950</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Diaconu, M.]]
[[Category: Diaconu, M.]]

Revision as of 01:59, 29 September 2014

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

Structural highlights

1zax is a 7 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:1zav, 1zaw
Gene:rplJ (Thermotoga maritima), rplL (Thermotoga maritima)
Resources:FirstGlance, OCA, RCSB, PDBsum

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

  1. ↑ 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

1zax, resolution 2.10Å

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