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| | <StructureSection load='1li7' size='340' side='right'caption='[[1li7]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1li7' size='340' side='right'caption='[[1li7]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1li7]] is a 2 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=1LI7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LI7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1li7]] is a 2 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=1LI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LI7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</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]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1li5|1li5]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</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/Cysteine--tRNA_ligase Cysteine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.16 6.1.1.16] </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=1li7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1li7 OCA], [https://pdbe.org/1li7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1li7 RCSB], [https://www.ebi.ac.uk/pdbsum/1li7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1li7 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=1li7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1li7 OCA], [http://pdbe.org/1li7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1li7 RCSB], [http://www.ebi.ac.uk/pdbsum/1li7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1li7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SYC_ECOLI SYC_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: Cysteine--tRNA ligase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hou, Y M]] | + | [[Category: Hou Y-M]] |
| - | [[Category: Newberry, K J]] | + | [[Category: Newberry KJ]] |
| - | [[Category: Perona, J J]] | + | [[Category: Perona JJ]] |
| - | [[Category: Cysteine]]
| + | |
| - | [[Category: E coli]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Trna synthetase]]
| + | |
| Structural highlights
Function
SYC_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
Cysteinyl-tRNA synthetase (CysRS) is highly specific for synthesis of cysteinyl adenylate, yet does not possess the amino acid editing activity characteristic of many other tRNA synthetases. To elucidate how CysRS is able to distinguish cysteine from non-cognate amino acids, crystal structures of the Escherichia coli enzyme were determined in apo and cysteine-bound states. The structures reveal that the substrate cysteine thiolate forms a single direct interaction with a zinc ion bound at the base of the active site cleft, in a trigonal bipyramidal geometry together with four highly conserved protein side chains. Cysteine binding induces movement of the zinc ion towards substrate, as well as flipping of the conserved Trp205 indole ring to pack on the thiol side chain. The imidazole groups of five conserved histidines lie adjacent to the zinc ion, forming a unique arrangement suggestive of functional significance. Thus, amino acid discrimination without editing arises most directly from the favorable zinc-thiolate interaction, which is not possible for non-cognate substrates. Additional selectivity may be generated during the induced-fit conformational changes that help assemble the active site.
Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase.,Newberry KJ, Hou YM, Perona JJ EMBO J. 2002 Jun 3;21(11):2778-87. PMID:12032090[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Newberry KJ, Hou YM, Perona JJ. Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase. EMBO J. 2002 Jun 3;21(11):2778-87. PMID:12032090 doi:http://dx.doi.org/10.1093/emboj/21.11.2778
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