5vh6
From Proteopedia
(Difference between revisions)
(New page: ==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' ...) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
==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]] 2.61Å' scene=''> | + | <StructureSection load='5vh6' size='340' side='right'caption='[[5vh6]], [[Resolution|resolution]] 2.61Å' 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 [ | + | <table><tr><td colspan='2'>[[5vh6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. 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 [https://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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.61Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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'>[https://proteopedia.org/fgij/fg.htm?mol=5vh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vh6 OCA], [https://pdbe.org/5vh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vh6 RCSB], [https://www.ebi.ac.uk/pdbsum/5vh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vh6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://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: | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Dubrovska | + | [[Category: Anderson WF]] |
| - | [[Category: Grimshaw | + | [[Category: Dubrovska I]] |
| - | [[Category: Kiryukhina | + | [[Category: Grimshaw S]] |
| - | [[Category: Kwon | + | [[Category: Kiryukhina O]] |
| - | [[Category: Minasov | + | [[Category: Kwon K]] |
| - | [[Category: Shuvalova | + | [[Category: Minasov G]] |
| - | + | [[Category: Shuvalova L]] | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
2.6 Angstrom Resolution Crystal Structure of N-terminal Fragment (residues 1-406) of Elongation Factor G from Bacillus subtilis.
| |||||||||||
