1PYS

PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

Summary for 1PYS

• Entry DOI: 10.2210/pdb1pys/pdb
• Descriptor: PHENYLALANYL-TRNA SYNTHETASE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: phenylalanyl-trna synthetase, class ii aminoacyl-trna synthetase, thermus thermophilus, rbd domain, sh3 domain, helix-turn-helix motif, aminoacyl-trna synthetase
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm: Q5SGX2 Q5SGX1
• Total number of polymer chains: 2
• Total formula weight: 126054.16

Authors

Safro, M.,Mosyak, L.,Goldgur, Y.,Reshetnikova, L.,Delarue, M. (deposition date: 1996-11-14, release date: 1997-11-19, Last modification date: 2024-02-14)

Primary citation

Mosyak, L.,Reshetnikova, L.,Goldgur, Y.,Delarue, M.,Safro, M.G.
Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.
Nat.Struct.Biol., 2:537-547, 1995

PubMed Abstract: The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains. The alpha beta heterodimer contains most of the building blocks so far identified in the class II synthetases. The presence of an RNA-binding domain, similar to that of the U1A spliceosomal protein, in the beta-subunit is indicative of structural relationships among different families of RNA-binding proteins. The structure suggests a plausible catalytic mechanism which explains why the primary site of tRNA aminoacylation is different from that of the other class II enzymes.

PubMed: 7664121
DOI: 10.1038/nsb0795-537

Experimental method

X-RAY DIFFRACTION (2.9 Å)