3foz
From Proteopedia
(Difference between revisions)
(8 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | {{Seed}} | ||
- | [[Image:3foz.png|left|200px]] | ||
- | < | + | ==Structure of E. coli Isopentenyl-tRNA transferase in complex with E. coli tRNA(Phe)== |
- | + | <StructureSection load='3foz' size='340' side='right'caption='[[3foz]], [[Resolution|resolution]] 2.50Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3foz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FOZ FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |
- | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=3foz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3foz OCA], [https://pdbe.org/3foz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3foz RCSB], [https://www.ebi.ac.uk/pdbsum/3foz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3foz ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/MIAA_ECOLI MIAA_ECOLI] Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).<ref>PMID:9012675</ref> <ref>PMID:9148919</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/3foz_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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/main_output.php?pdb_ID=3foz ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | tRNAs that read codons starting with U are usually modified at their A37 by isopentenyl-tRNA transferases in order to minimize peptidyl-tRNA slippage in translation. The consensus substrate requirements of E. coli's isopentenyl-tRNA transferase, MiaA, have been the focus of extensive study. However, the molecular basis of tRNA-MiaA recognition remains unknown. Here, we describe the 2.5 A crystal structure of MiaA in complex with substrate tRNA(Phe). Comparative structural analysis reveals that the enzymatic reaction involves an RNA-protein mutually induced fit mechanism in which large domain movements in MiaA provoke the partial unfolding of the substrate tRNA anticodon loop. In addition, we show how substrate tRNAs are recognized by MiaA through a combination of direct and indirect sequence readouts. | ||
- | + | RNA-protein mutually induced Fit: Structure of E. coli isopentenyl-tRNA transferase in complex with tRNA(Phe).,Seif E, Hallberg BM J Biol Chem. 2009 Jan 21. PMID:19158097<ref>PMID:19158097</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 3foz" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Escherichia coli]] |
- | + | [[Category: Escherichia coli K-12]] | |
- | + | [[Category: Large Structures]] | |
- | == | + | [[Category: Hallberg BM]] |
- | + | [[Category: Seif E]] | |
- | [[Category: Escherichia coli | + | |
- | [[Category: | + | |
- | + | ||
- | + | ||
- | + | ||
- | [[Category: | + | |
- | [[Category: | + | |
- | [[Category: | + | |
- | + | ||
- | + | ||
- | + |
Current revision
Structure of E. coli Isopentenyl-tRNA transferase in complex with E. coli tRNA(Phe)
|