1qu2: Difference between revisions

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[[Image:1qu2.gif|left|200px]]
{{Seed}}
[[Image:1qu2.png|left|200px]]


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{{STRUCTURE_1qu2|  PDB=1qu2  |  SCENE=  }}  
{{STRUCTURE_1qu2|  PDB=1qu2  |  SCENE=  }}  


'''INSIGHTS INTO EDITING FROM AN ILE-TRNA SYNTHETASE STRUCTURE WITH TRNA(ILE) AND MUPIROCIN'''
===INSIGHTS INTO EDITING FROM AN ILE-TRNA SYNTHETASE STRUCTURE WITH TRNA(ILE) AND MUPIROCIN===




==Overview==
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Isoleucyl-transfer RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at its synthetic active site and hydrolyzes incorrectly acylated amino acids at its editing active site. The 2.2 angstrom resolution crystal structure of Staphylococcus aureus IleRS complexed with tRNA(Ile) and Mupirocin shows the acceptor strand of the tRNA(Ile) in the continuously stacked, A-form conformation with the 3' terminal nucleotide in the editing active site. To position the 3' terminus in the synthetic active site, the acceptor strand must adopt the hairpinned conformation seen in tRNA(Gln) complexed with its synthetase. The amino acid editing activity of the IleRS may result from the incorrect products shuttling between the synthetic and editing active sites, which is reminiscent of the editing mechanism of DNA polymerases.
The line below this paragraph, {{ABSTRACT_PUBMED_10446055}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10446055 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10446055}}


==About this Structure==
==About this Structure==
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[[Category: Metal ion]]
[[Category: Metal ion]]
[[Category: Protein-rna complex]]
[[Category: Protein-rna complex]]
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