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| {{STRUCTURE_1jij| PDB=1jij | SCENE= }} | | {{STRUCTURE_1jij| PDB=1jij | SCENE= }} |
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| '''Crystal structure of S. aureus TyrRS in complex with SB-239629'''
| | ===Crystal structure of S. aureus TyrRS in complex with SB-239629=== |
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| ==Overview==
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| SB-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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11567092}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11567092 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11567092}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Truncation]] | | [[Category: Truncation]] |
| [[Category: Tyrosyl-trna synthetase]] | | [[Category: Tyrosyl-trna synthetase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:15:57 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:18:00 2008'' |