4R3Z

Crystal structure of human ArgRS-GlnRS-AIMP1 complex

Summary for 4R3Z

• Entry DOI: 10.2210/pdb4r3z/pdb
• Descriptor: Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Arginine--tRNA ligase, cytoplasmic, Glutamine--tRNA ligase (3 entities in total)
• Functional Keywords: amino-acyl trna synthetase complex, multi-synthetase complex, ligation amino acid to trna, protein binding-ligase complex, protein binding/ligase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q12904; Cytoplasm : P54136 P47897
• Total number of polymer chains: 3
• Total formula weight: 202155.03

Authors

Fu, Y.,Kim, Y.,Cho, Y. (deposition date: 2014-08-18, release date: 2014-10-08, Last modification date: 2024-03-20)

Primary citation

Fu, Y.,Kim, Y.,Jin, K.S.,Kim, H.S.,Kim, J.H.,Wang, D.M.,Park, M.,Jo, C.H.,Kwon, N.H.,Kim, D.,Kim, M.H.,Jeon, Y.H.,Hwang, K.Y.,Kim, S.,Cho, Y.
Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation
Proc.Natl.Acad.Sci.USA, 111:15084-15089, 2014

PubMed Abstract: In higher eukaryotes, one of the two arginyl-tRNA synthetases (ArgRSs) has evolved to have an extended N-terminal domain that plays a crucial role in protein synthesis and cell growth and in integration into the multisynthetase complex (MSC). Here, we report a crystal structure of the MSC subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43. In this complex, the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. Mutation of AIMP1 destabilized the N-terminal helix of ArgRS and abrogated its catalytic activity. Mutation of the N-terminal helix of ArgRS liberated GlnRS, which is known to control cell death. This ternary complex was further anchored to AIMP2/p38 through interaction with AIMP1. These findings demonstrate the importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC protein complex.

PubMed: 25288775
DOI: 10.1073/pnas.1408836111

Experimental method

X-RAY DIFFRACTION (4.033 Å)