1jil: Difference between revisions
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<StructureSection load='1jil' size='340' side='right'caption='[[1jil]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1jil' size='340' side='right'caption='[[1jil]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jil]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1jil]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JIL FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=485:[2-AMINO-3-(4-HYDROXY-PHENYL)-PROPIONYLAMINO]-+(3,4,5-TRIHYDROXY-6-METHYL-TETRAHYDRO-PYRAN-2-YL)-+ACETIC+ACID'>485</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=1jil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jil OCA], [https://pdbe.org/1jil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jil RCSB], [https://www.ebi.ac.uk/pdbsum/1jil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jil 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=1jil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jil OCA], [https://pdbe.org/1jil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jil RCSB], [https://www.ebi.ac.uk/pdbsum/1jil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jil ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SYY_STAAE SYY_STAAE] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).[HAMAP-Rule:MF_02006] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: | [[Category: Janson CA]] | ||
[[Category: | [[Category: Jarvest RL]] | ||
[[Category: | [[Category: Qiu X]] | ||
[[Category: Smith WW]] | |||
Latest revision as of 11:41, 16 August 2023
Crystal structure of S. aureus TyrRS in complex with SB284485Crystal structure of S. aureus TyrRS in complex with SB284485
Structural highlights
FunctionSYY_STAAE Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).[HAMAP-Rule:MF_02006] 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 PubMedSB-219383 and its analogues are a class of potent and specific inhibitors of bacterial tyrosyl-tRNA synthetases. Crystal structures of these inhibitors have been solved in complex with the tyrosyl-tRNA synthetase from Staphylococcus aureus, the bacterium that is largely responsible for hospital-acquired infections. The full-length enzyme yielded crystals that diffracted to 2.8 A resolution, but a truncated version of the enzyme allowed the resolution to be extended to 2.2 A. These inhibitors not only occupy the known substrate binding sites in unique ways, but also reveal a butyl binding pocket. It was reported that the Bacillus stearothermophilus TyrRS T51P mutant has much increased catalytic activity. The S. aureus enzyme happens to have a proline at position 51. Therefore, our structures may contribute to the understanding of the catalytic mechanism and provide the structural basis for designing novel antimicrobial agents. Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors.,Qiu X, Janson CA, Smith WW, Green SM, McDevitt P, Johanson K, Carter P, Hibbs M, Lewis C, Chalker A, Fosberry A, Lalonde J, Berge J, Brown P, Houge-Frydrych CS, Jarvest RL Protein Sci. 2001 Oct;10(10):2008-16. PMID:11567092[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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