2qk4

Human glycinamide ribonucleotide synthetase

spinqualitylabelsall models 2qk4, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qk4 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, CL, GOL, SO4 Gene: GART, PGFT, PRGS (HUMAN) Activity: Phosphoribosylamine--glycine ligase, with EC number 6.3.4.13 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural studies of tri-functional human GART.,Welin M, Grossmann JG, Flodin S, Nyman T, Stenmark P, Tresaugues L, Kotenyova T, Johansson I, Nordlund P, Lehtio L Nucleic Acids Res. 2010 Nov 1;38(20):7308-19. Epub 2010 Jul 14. PMID:20631005 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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