1h4t: Difference between revisions
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[[Category: class ii aminoacyl-trna synthetase]] | [[Category: class ii aminoacyl-trna synthetase]] | ||
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Revision as of 16:23, 30 October 2007
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PROLYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH L-PROLINE
OverviewOverview
We describe the recognition by Thermus thermophilus prolyl-tRNA synthetase, (ProRSTT) of proline, ATP and prolyl-adenylate and the sequential, conformational changes occurring when the substrates bind and the, activated intermediate is formed. Proline and ATP binding cause, respectively conformational changes in the proline binding loop and motif, 2 loop. However formation of the activated intermediate is necessary for, the final conformational ordering of a ten residue peptide ("ordering, loop") close to the active site which would appear to be essential for, functional tRNA 3' end binding. These induced fit conformational changes, ensure that the enzyme is highly specific for proline activation and, aminoacylation. We also present new structures of apo and AMP bound, histidyl-tRNA ... [(full description)]
About this StructureAbout this Structure
1H4T is a [Single protein] structure of sequence from [Thermus thermophilus] with ZN and PRO as [ligands]. Active as [Proline--tRNA ligase], with EC number [6.1.1.15]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7 and AC8. Full crystallographic information is available from [OCA].
ReferenceReference
A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyl-tRNA synthetase: comparison with histidyl-tRNA synthetase., Yaremchuk A, Tukalo M, Grotli M, Cusack S, J Mol Biol. 2001 Jun 15;309(4):989-1002. PMID:11399074
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