9nl5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==E. coli pre-elongation complex without an A-site tRNA with EQ2-EttA in Hydrolytic 1 conformation== | |
| - | + | <StructureSection load='9nl5' size='340' side='right'caption='[[9nl5]], [[Resolution|resolution]] 3.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9nl5]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9NL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9NL5 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | [[Category: Hunt | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9nl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9nl5 OCA], [https://pdbe.org/9nl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9nl5 RCSB], [https://www.ebi.ac.uk/pdbsum/9nl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9nl5 ProSAT]</span></td></tr> |
| - | [[Category: Singh | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RL1_ECOLI RL1_ECOLI] One of the primary rRNA binding proteins, it binds very close to the 3'-end of the 23S rRNA. Forms part of the L1 stalk. It is often not seen in high-resolution crystal structures, but can be seen in cryo_EM and 3D reconstruction models. These indicate that the distal end of the stalk moves by approximately 20 angstroms (PubMed:12859903). This stalk movement is thought to be coupled to movement of deacylated tRNA into and out of the E site, and thus to participate in tRNA translocation (PubMed:12859903). Contacts the P and E site tRNAs.[HAMAP-Rule:MF_01318_B] Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.[HAMAP-Rule:MF_01318_B] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hunt JF]] | ||
| + | [[Category: Singh S]] | ||
Current revision
E. coli pre-elongation complex without an A-site tRNA with EQ2-EttA in Hydrolytic 1 conformation
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