1hc7
From Proteopedia
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PROLYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS
Overview
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 Structure
1HC7 is a [Single protein] structure of sequence from [Thermus thermophilus] with ZN as [ligand]. Active as [Proline--tRNA ligase], with EC number [6.1.1.15]. Structure known Active Sites: ZN1, ZN2, ZN3 and ZN4. Full crystallographic information is available from [OCA].
Reference
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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