1zax

<StructureSection load='1zax' size='340' side='right' caption='[[1zax]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[1zax]] 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=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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zav|1zav]], [[1zaw|1zaw]]</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'>[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://pdbe.org/1zax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zax RCSB], [http://www.ebi.ac.uk/pdbsum/1zax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zax ProSAT]</span></td></tr>

[[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.

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== 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.

 

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== References ==

<references/>

[[Category: Atcc 43589]]

[[Category: Diaconu, M]]

[[Category: Fischer, N]]

[[Category: Harms, J M]]

[[Category: Kothe, U]]

[[Category: Rodnina, M V]]

[[Category: Schluenzen, F]]

[[Category: Stark, H]]

[[Category: Tonevitski, A G]]

[[Category: Wahl, M C]]

[[Category: Translation factor recruitment]]