2QK4

Human glycinamide ribonucleotide synthetase

2QK4 の概要

• エントリーDOI: 10.2210/pdb2qk4/pdb
• 分子名称: Trifunctional purine biosynthetic protein adenosine-3, CHLORIDE ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: purine synthesis, enzyme, protein-atp complex, structural genomics, structural genomics consortium, sgc, ligase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 98198.45

構造登録者

Lehtio, L.,Welin, M.,Arrowsmith, C.H.,Berglund, H.,Busam, R.,Collins, R.,Dahlgren, L.G.,Herman, M.D.,Edwards, A.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Hallberg, B.M.,Holmberg-Schiavone, L.,Johansson, I.,Kallas, A.,Karlberg, T.,Kotenyova, T.,Moche, M.,Nyman, T.,Persson, C.,Sagemark, J.,Stenmark, P.,Sundstrom, M.,Thorsell, A.G.,Tresaugues, L.,van den Berg, S.,Weigelt, J.,Nordlund, P.,Structural Genomics Consortium (SGC) (登録日: 2007-07-10, 公開日: 2007-07-24, 最終更新日: 2023-08-30)

主引用文献

Welin, M.,Grossmann, J.G.,Flodin, S.,Nyman, T.,Stenmark, P.,Tresaugues, L.,Kotenyova, T.,Johansson, I.,Nordlund, P.,Lehtio, L.
Structural studies of tri-functional human GART.
Nucleic Acids Res., 38:7308-7319, 2010

PubMed Abstract: Human purine de novo synthesis pathway contains several multi-functional enzymes, one of which, tri-functional GART, contains three enzymatic activities in a single polypeptide chain. We have solved structures of two domains bearing separate catalytic functions: glycinamide ribonucleotide synthetase and aminoimidazole ribonucleotide synthetase. Structures are compared with those of homologous enzymes from prokaryotes and analyzed in terms of the catalytic mechanism. We also report small angle X-ray scattering models for the full-length protein. These models are consistent with the enzyme forming a dimer through the middle domain. The protein has an approximate seesaw geometry where terminal enzyme units display high mobility owing to flexible linker segments. This resilient seesaw shape may facilitate internal substrate/product transfer or forwarding to other enzymes in the pathway.

PubMed: 20631005
DOI: 10.1093/nar/gkq595

実験手法

X-RAY DIFFRACTION (2.45 Å)