1ZQ1

Structure of GatDE tRNA-Dependent Amidotransferase from Pyrococcus abyssi

Summary for 1ZQ1

• Entry DOI: 10.2210/pdb1zq1/pdb
• Descriptor: Glutamyl-tRNA(Gln) amidotransferase subunit D, Glutamyl-tRNA(Gln) amidotransferase subunit E, ASPARTIC ACID, ... (4 entities in total)
• Functional Keywords: x-ray; 3d structure; asparaginase 1 family; gatd subfamily, lyase
• Biological source: Pyrococcus abyssi; More
• Total number of polymer chains: 4
• Total formula weight: 243526.36

Authors

Schmitt, E.,Panvert, M.,Blanquet, S.,Mechulam, Y. (deposition date: 2005-05-18, release date: 2005-10-18, Last modification date: 2024-10-30)

Primary citation

Schmitt, E.,Panvert, M.,Blanquet, S.,Mechulam, Y.
Structural Basis for tRNA-Dependent Amidotransferase Function
Structure, 13:1421-1433, 2005

PubMed Abstract: Besides direct charging of tRNAs by aminoacyl-tRNA synthetases, indirect routes also ensure attachment of some amino acids onto tRNA. Such routes may explain how new amino acids entered into protein synthesis. In archaea and in most bacteria, tRNA(Gln) is first misaminoacylated by glutamyl-tRNA synthetase. Glu-tRNA(Gln) is then matured into Gln-tRNA(Gln) by a tRNA-dependent amidotransferase. We report the structure of a tRNA-dependent amidotransferase-that of GatDE from Pyrococcus abyssi. The 3.0 A resolution crystal structure shows a tetramer with two GatD molecules as the core and two GatE molecules at the periphery. The fold of GatE cannot be related to that of any tRNA binding enzyme. The ammonium donor site on GatD and the tRNA site on GatE are markedly distant. Comparison of GatD and L-asparaginase structures shows how the motion of a beta hairpin region containing a crucial catalytic threonine may control the overall reaction cycle of GatDE.

PubMed: 16216574
DOI: 10.1016/j.str.2005.06.016

Experimental method

X-RAY DIFFRACTION (3 Å)