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==2.6 Angstrom Resolution Crystal Structure of N-terminal Fragment (residues 1-406) of Elongation Factor G from Bacillus subtilis.==
==2.6 Angstrom Resolution Crystal Structure of N-terminal Fragment (residues 1-406) of Elongation Factor G from Bacillus subtilis.==
<StructureSection load='5vh6' size='340' side='right' caption='[[5vh6]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
<StructureSection load='5vh6' size='340' side='right'caption='[[5vh6]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5vh6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VH6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VH6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5vh6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VH6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5VH6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=5vh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vh6 OCA], [http://pdbe.org/5vh6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vh6 RCSB], [http://www.ebi.ac.uk/pdbsum/5vh6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vh6 ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fusA, fus, BSU01120 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5vh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vh6 OCA], [http://pdbe.org/5vh6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vh6 RCSB], [http://www.ebi.ac.uk/pdbsum/5vh6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vh6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EFG_BACSU EFG_BACSU]] 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 (By similarity).  
[[http://www.uniprot.org/uniprot/EFG_BACSU EFG_BACSU]] 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 (By similarity).  
==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacsu]]
[[Category: Large Structures]]
[[Category: Anderson, W F]]
[[Category: Anderson, W F]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]