3L4G

Crystal structure of Homo Sapiens cytoplasmic Phenylalanyl-tRNA synthetase

Summary for 3L4G

• Entry DOI: 10.2210/pdb3l4g/pdb
• Descriptor: Phenylalanyl-tRNA synthetase alpha chain, Phenylalanyl-tRNA synthetase beta chain, PHENYLALANINE (3 entities in total)
• Functional Keywords: aminoacylation, trna-binding, dna-binding domain, four-helix bundle, acetylation, aminoacyl-trna synthetase, atp-binding, cytoplasm, ligase, nucleotide-binding, phosphoprotein, polymorphism, protein biosynthesis
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm (By similarity): Q9Y285 Q9NSD9
• Total number of polymer chains: 16
• Total formula weight: 992193.60

Authors

Finarov, I.,Moor, N.,Kessler, N.,Klipcan, L.,Safro, M.G. (deposition date: 2009-12-20, release date: 2010-03-09, Last modification date: 2023-11-01)

Primary citation

Finarov, I.,Moor, N.,Kessler, N.,Klipcan, L.,Safro, M.G.
Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for kingdom-specific design of the active sites and tRNA binding patterns.
Structure, 18:343-353, 2010

PubMed Abstract: The existence of three types of phenylalanyl-tRNA synthetase (PheRS), bacterial (alphabeta)(2), eukaryotic/archaeal cytosolic (alphabeta)(2), and mitochondrial alpha, is a prominent example of structural diversity within the aaRS family. PheRSs have considerably diverged in primary sequences, domain compositions, and subunit organizations. Loss of the anticodon-binding domain B8 in human cytosolic PheRS (hcPheRS) is indicative of variations in the tRNA(Phe) binding and recognition as compared to bacterial PheRSs. We report herein the crystal structure of hcPheRS in complex with phenylalanine at 3.3 A resolution. A novel structural module has been revealed at the N terminus of the alpha subunit. It stretches out into the solvent of approximately 80 A and is made up of three structural domains (DBDs) possessing DNA-binding fold. The dramatic reduction of aminoacylation activity for truncated N terminus variants coupled with structural data and tRNA-docking model testify that DBDs play crucial role in hcPheRS activity.

PubMed: 20223217
DOI: 10.1016/j.str.2010.01.002

Experimental method

X-RAY DIFFRACTION (3.3 Å)