2bcw

<StructureSection load='2bcw' size='340' side='right' caption='[[2bcw]], [[Resolution|resolution]] 11.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[2bcw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BCW FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mms|1mms]], [[1ctf|1ctf]], [[1elo|1elo]]</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=2bcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bcw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bcw RCSB], [http://www.ebi.ac.uk/pdbsum/2bcw PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/RL11_THEMA RL11_THEMA]] This protein binds directly to 23S ribosomal RNA. [[http://www.uniprot.org/uniprot/EFG_THETH EFG_THETH]] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. [[http://www.uniprot.org/uniprot/RL7_ECOLI RL7_ECOLI]] Seems to be the binding site for several of the factors involved in protein synthesis and appears to be essential for accurate translation.[HAMAP-Rule:MF_00368]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/2bcw_consurf.spt"</scriptWhenChecked>

</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="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

During tRNA translocation on the ribosome, an arc-like connection (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal subunit in the GDP state. To delineate the boundary of EF-G within the ALC, we tagged an amino acid residue near the tip of the G' domain of EF-G with undecagold, which was then visualized with three-dimensional cryo-electron microscopy (cryo-EM). Two distinct positions for the undecagold, observed in the GTP-state and GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labeled amino acid. Molecular analyses of the cryo-EM maps show: (1) that three structural components, the N-terminal domain of ribosomal protein L11, the C-terminal domain of ribosomal protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC; and (2) that both EF-G and the ribosomal protein L7/L12 undergo large conformational changes to form the ALC.

Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM.,Datta PP, Sharma MR, Qi L, Frank J, Agrawal RK Mol Cell. 2005 Dec 9;20(5):723-31. PMID:16337596<ref>PMID:16337596</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

*[[Elongation factor|Elongation factor]]

*[[Ribosomal protein L7|Ribosomal protein L7]]

<references/>

</StructureSection>

[[Category: Agrawal, R K]]

[[Category: Datta, P P]]

[[Category: Frank, J]]

[[Category: Qi, L]]

[[Category: Sharma, M R]]

[[Category: Ribosome]]