1GPJ

Glutamyl-tRNA Reductase from Methanopyrus kandleri

1GPJ の概要

• エントリーDOI: 10.2210/pdb1gpj/pdb
• 分子名称: Glutamyl-tRNA reductase, GLUTAMIC ACID, (2R,3R,4S,5S)-4-AMINO-2-[6-(DIMETHYLAMINO)-9H-PURIN-9-YL]-5-(HYDROXYMETHYL)TETRAHYDRO-3-FURANOL, ... (5 entities in total)
• 機能のキーワード: reductase, trna-dependent tetrapyrrole biosynthesis, glutamyl trna- reductase
• 由来する生物種: Methanopyrus kandleri
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46073.08

構造登録者

Moser, J.,Schubert, W.-D.,Beier, V.,Bringemeier, I.,Jahn, D.,Heinz, D.W. (登録日: 2001-11-05, 公開日: 2002-01-04, 最終更新日: 2024-05-08)

主引用文献

Moser, J.,Schubert, W.D.,Beier, V.,Bringemeier, I.,Jahn, D.,Heinz, D.W.
V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis.
EMBO J., 20:6583-6590, 2001

PubMed Abstract: Processes vital to life such as respiration and photosynthesis critically depend on the availability of tetrapyrroles including hemes and chlorophylls. tRNA-dependent catalysis generally is associated with protein biosynthesis. An exception is the reduction of glutamyl-tRNA to glutamate-1-semialdehyde by the enzyme glutamyl-tRNA reductase. This reaction is the indispensable initiating step of tetrapyrrole biosynthesis in plants and most prokaryotes. The crystal structure of glutamyl-tRNA reductase from the archaeon Methanopyrus kandleri in complex with the substrate-like inhibitor glutamycin at 1.9 A resolution reveals an extended yet planar V-shaped dimer. The well defined interactions of the inhibitor with the active site support a thioester-mediated reduction process. Modeling the glutamyl-tRNA onto each monomer reveals an extensive protein-tRNA interface. We furthermore propose a model whereby the large void of glutamyl-tRNA reductase is occupied by glutamate-1-semialdehyde-1,2-mutase, the subsequent enzyme of this pathway, allowing for the efficient synthesis of 5-aminolevulinic acid, the common precursor of all tetrapyrroles.

PubMed: 11726494
DOI: 10.1093/emboj/20.23.6583

実験手法

X-RAY DIFFRACTION (1.95 Å)