1zb4: Difference between revisions
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{{Theoretical_model}} | {{Theoretical_model}} | ||
< | ==N-TERMINAL DOMAIN OF HMAL10.== | ||
The | <StructureSection load='1zb4' size='340' side='right'caption='[[1zb4]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZB4 FirstGlance]. <br> | |||
</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=1zb4 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1zb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zb4 ProSAT]</span></td></tr> | |||
</table> | |||
<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 1zb4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Theoretical Model]] | ||
[[Category: Large Structures]] | |||
== | |||
< | |||
[[Category: Diaconu, M]] | [[Category: Diaconu, M]] | ||
[[Category: Fischer, N]] | [[Category: Fischer, N]] | ||
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[[Category: Tonevitsky, A G]] | [[Category: Tonevitsky, A G]] | ||
[[Category: Wahl, M C]] | [[Category: Wahl, M C]] | ||
Latest revision as of 11:18, 10 November 2021
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N-TERMINAL DOMAIN OF HMAL10.N-TERMINAL DOMAIN OF HMAL10.
Structural highlights
Publication Abstract from PubMedThe 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. References
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