2V9Y

Human aminoimidazole ribonucleotide synthetase

Summary for 2V9Y

• Entry DOI: 10.2210/pdb2v9y/pdb
• Related: 1MEJ 1MEN 1MEO 1NJS 1ZLX 1ZLY
• Descriptor: PHOSPHORIBOSYLFORMYLGLYCINAMIDINE CYCLO-LIGASE, SULFATE ION (3 entities in total)
• Functional Keywords: multifunctional enzyme, structural genomics consortium, nucleotide-binding, purine biosynthesis, sgc, airs, gart, ligase, transferase, atp-binding, aminoimidazole ribonucleotide synthetase, phosphorylation, purine metabolism, structural genomics
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 71948.22

Authors

Welin, M.,Lehtio, L.,Arrowsmith, C.H.,Berglund, H.,Busam, R.,Collins, R.,Dahlgren, L.G.,Herman, M.D.,Edwards, A.M.,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) (deposition date: 2007-08-28, release date: 2007-09-11, Last modification date: 2023-12-13)

Primary citation

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-, 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

Experimental method

X-RAY DIFFRACTION (2.1 Å)