2iy5

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Revision as of 17:43, 29 October 2007

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spinqualitylabelsall models 2iy5, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TRNA AND A PHENYLALANYL-ADENYLATE ANALOG

Overview

The crystal structure of the ternary complex of (alphabeta)(2), heterotetrameric phenylalanyl-tRNA synthetase (PheRS) from Thermus, thermophilus with cognate tRNA(Phe) and a nonhydrolyzable, phenylalanyl-adenylate analogue (PheOH-AMP) has been determined at 3.1 A, resolution. It reveals conformational changes in tRNA(Phe) induced by the, PheOH-AMP binding. The single-stranded 3' end exhibits a hairpin, conformation in contrast to the partial unwinding observed previously in, the binary PheRS.tRNA(Phe) complex. The CCA end orientation is stabilized, by extensive base-specific interactions of A76 and C75 with the protein, and by intra-RNA interactions of A73 with adjacent nucleotides. The, 4-amino group of the "bulged out" C75 is trapped by two negatively charged, residues of the beta ... [(full description)]

About this Structure

2IY5 is a [Protein complex] structure of sequences from [Thermus thermophilus] with MG and FYA as [ligands]. Active as [[1]], with EC number [6.1.1.20]. Full crystallographic information is available from [OCA].

Reference

The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end., Moor N, Kotik-Kogan O, Tworowski D, Sukhanova M, Safro M, Biochemistry. 2006 Sep 5;45(35):10572-83. PMID:16939209

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