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| | <StructureSection load='1kog' size='340' side='right'caption='[[1kog]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='1kog' size='340' side='right'caption='[[1kog]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kog]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KOG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kog]] is a 16 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=1KOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSB:5-O-(N-(L-THREONYL)-SULFAMOYL)ADENOSINE'>TSB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1evl|1evl]], [[1qf6|1qf6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TSB:5-O-(N-(L-THREONYL)-SULFAMOYL)ADENOSINE'>TSB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </span></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=1kog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kog OCA], [https://pdbe.org/1kog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kog RCSB], [https://www.ebi.ac.uk/pdbsum/1kog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kog ProSAT]</span></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=1kog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kog OCA], [http://pdbe.org/1kog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kog RCSB], [http://www.ebi.ac.uk/pdbsum/1kog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kog ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SYT_ECOLI SYT_ECOLI]] ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184] | + | [https://www.uniprot.org/uniprot/SYT_ECOLI SYT_ECOLI] ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Threonine--tRNA ligase]]
| + | [[Category: Caillet J]] |
| - | [[Category: Caillet, J]] | + | [[Category: Dock-Bregeon AC]] |
| - | [[Category: Dock-Bregeon, A C]] | + | [[Category: Ehresmann B]] |
| - | [[Category: Ehresmann, B]] | + | [[Category: Ehresmann C]] |
| - | [[Category: Ehresmann, C]] | + | [[Category: Moras D]] |
| - | [[Category: Moras, D]] | + | [[Category: Rees B]] |
| - | [[Category: Rees, B]] | + | [[Category: Romby P]] |
| - | [[Category: Romby, P]] | + | [[Category: Sankaranarayanan R]] |
| - | [[Category: Sankaranarayanan, R]] | + | [[Category: Springer M]] |
| - | [[Category: Springer, M]] | + | [[Category: Torres-Larrios A]] |
| - | [[Category: Torres-Larrios, A]] | + | |
| - | [[Category: Ligase-rna complex]]
| + | |
| - | [[Category: Protein-rna complex]]
| + | |
| - | [[Category: Rna base triple]]
| + | |
| - | [[Category: Rna double helix]]
| + | |
| - | [[Category: Rna stem-loop]]
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| Structural highlights
Function
SYT_ECOLI ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Escherichia coli threonyl-tRNA synthetase (ThrRS) represses the translation of its own messenger RNA by binding to an operator located upstream of the initiation codon. The crystal structure of the complex between the core of ThrRS and the essential domain of the operator shows that the mRNA uses the recognition mode of the tRNA anticodon loop to initiate binding. The final positioning of the operator, upon which the control mechanism is based, relies on a characteristic RNA motif adapted to the enzyme surface. The finding of other thrS operators that have this conserved motif leads to a generalization of this regulatory mechanism to a subset of Gram-negative bacteria.
Structural basis of translational control by Escherichia coli threonyl tRNA synthetase.,Torres-Larios A, Dock-Bregeon AC, Romby P, Rees B, Sankaranarayanan R, Caillet J, Springer M, Ehresmann C, Ehresmann B, Moras D Nat Struct Biol. 2002 May;9(5):343-7. PMID:11953757[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Torres-Larios A, Dock-Bregeon AC, Romby P, Rees B, Sankaranarayanan R, Caillet J, Springer M, Ehresmann C, Ehresmann B, Moras D. Structural basis of translational control by Escherichia coli threonyl tRNA synthetase. Nat Struct Biol. 2002 May;9(5):343-7. PMID:11953757 doi:10.1038/nsb789
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