3CMQ

Crystal structure of human mitochondrial phenylalanine tRNA synthetase

Summary for 3CMQ

• Entry DOI: 10.2210/pdb3cmq/pdb
• Related: 1pys
• Descriptor: Phenylalanyl-tRNA synthetase, mitochondrial, MAGNESIUM ION, ADENOSINE-5'-[PHENYLALANINYL-PHOSPHATE], ... (4 entities in total)
• Functional Keywords: classii aarss fold, rrm domain, trna, rna recogntion, aminoacyl-trna synthetase, atp-binding, ligase, mitochondrion, nucleotide-binding, protein biosynthesis, transit peptide
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 49024.74

Authors

Klipcan, L.,Levin, I.L.,Kessler, N.,Moor, N.,Finarov, I.,Safro, M. (deposition date: 2008-03-24, release date: 2008-07-01, Last modification date: 2023-08-30)

Primary citation

Klipcan, L.,Levin, I.,Kessler, N.,Moor, N.,Finarov, I.,Safro, M.
The tRNA-Induced Conformational Activation of Human Mitochondrial Phenylalanyl-tRNA Synthetase.
Structure, 16:1095-1104, 2008

PubMed Abstract: All class II aminoacyl-tRNA synthetases (aaRSs) are known to be active as functional homodimers, homotetramers, or heterotetramers. However, multimeric organization is not a prerequisite for phenylalanylation activity, as monomeric mitochondrial phenylalanyl-tRNA synthetase (PheRS) is also active. We herein report the structure, at 2.2 A resolution, of a human monomeric mitPheRS complexed with Phe-AMP. The smallest known aaRS, which is, in fact, 1/5 of a cytoplasmic analog, is a chimera of the catalytic module of the alpha and anticodon binding domain (ABD) of the bacterial beta subunit of (alphabeta)2 PheRS. We demonstrate that the ABD located at the C terminus of mitPheRS overlaps with the acceptor stem of phenylalanine transfer RNA (tRNAPhe) if the substrate is positioned in a manner similar to that seen in the binary Thermus thermophilus complex. Thus, formation of the PheRS-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement (hinge-type rotation through approximately 160 degrees) of the ABD upon tRNA binding.

PubMed: 18611382
DOI: 10.1016/j.str.2008.03.020

Experimental method

X-RAY DIFFRACTION (2.2 Å)