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| | ==SOLUTION STRUCTURE OF THE ANTICODON BINDING DOMAIN OF ESCHERICHIA COLI LYSYL-TRNA SYNTHETASE AND STUDIES OF ITS INTERACTIONS WITH TRNA-LYS== | | ==SOLUTION STRUCTURE OF THE ANTICODON BINDING DOMAIN OF ESCHERICHIA COLI LYSYL-TRNA SYNTHETASE AND STUDIES OF ITS INTERACTIONS WITH TRNA-LYS== |
| - | <StructureSection load='1krt' size='340' side='right'caption='[[1krt]], [[NMR_Ensembles_of_Models | 9 NMR models]]' scene=''> | + | <StructureSection load='1krt' size='340' side='right'caption='[[1krt]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1krt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KRT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1krt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KRT FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1krs|1krs]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LYSS CODONS 40 - 149 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1krt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1krt OCA], [https://pdbe.org/1krt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1krt RCSB], [https://www.ebi.ac.uk/pdbsum/1krt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1krt ProSAT]</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=1krt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1krt OCA], [https://pdbe.org/1krt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1krt RCSB], [https://www.ebi.ac.uk/pdbsum/1krt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1krt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SYK1_ECOLI SYK1_ECOLI] |
| | == 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: Lysine--tRNA ligase]]
| + | [[Category: Commans S]] |
| - | [[Category: Commans, S]] | + | [[Category: Dardel F]] |
| - | [[Category: Dardel, F]] | + | |
| - | [[Category: Aminoacyl-trna synthetase]]
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| Structural highlights
Function
SYK1_ECOLI
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
A protein domain corresponding to residues 31 to 149 of the E. coli Lysyl-tRNA synthetase species corresponding to the lysS gene was expressed and 15N-labelled. 1H and 15N NMR resonance assignments for this domain were obtained by two-dimensional and three-dimensional homonuclear and heteronuclear spectroscopy. Using distance geometry and simulated annealing, a three-dimensional structure could be calculated using 701 NOE and 86 dihedral angle restraints. It is composed of a five-stranded antiparallel beta-barrel capped by three alpha-helices at its ends. This structure closely resembles that of the N-terminal domain of the other E. coli lysyl-tRNA synthetase species expressed from the lysU gene and is highly homologous to the fold observed for the corresponding region of aspartyl-tRNA synthetase. It is shown that the isolated N-terminal fragment of lysyl-tRNA synthetase can interact with tRNA(Lys) as well as with poly (U), which mimics the anticodon sequence. Amino acid residues involved in these interactions were identified and, in the case of poly-U, a number of specific protein-RNA contacts were characterized. Specific recognition of tRNA(Lys) involves a cluster of four structurally well-defined aromatic residues, anchored on the beta-strands, and basic residues located on the surrounding loops. This organization is reminiscent of other RNA binding proteins, such as the U1A small nuclear ribonucleoprotein.
Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys).,Commans S, Plateau P, Blanquet S, Dardel F J Mol Biol. 1995 Oct 13;253(1):100-13. PMID:7473706[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Commans S, Plateau P, Blanquet S, Dardel F. Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys). J Mol Biol. 1995 Oct 13;253(1):100-13. PMID:7473706 doi:http://dx.doi.org/10.1006/jmbi.1995.0539
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