1mf1 | pdb_00001mf1

Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with AMP

spinqualitylabelsall models 1mf1, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mf1 is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, AMP Related: 1mez, 1mf0 Gene: Adss1 (LK3 transgenic mice) Activity: Adenylosuccinate synthase, with EC number 6.3.4.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PURA1_MOUSE] Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. 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 Adenylosuccinate synthetase governs the committed step of AMP biosynthesis, the generation of 6-phosphoryl-IMP from GTP and IMP followed by the formation of adenylosuccinate from 6-phosphoryl-IMP and l-aspartate. The enzyme is subject to feedback inhibition by AMP and adenylosuccinate, but crystallographic complexes of the mouse muscle synthetase presented here infer mechanisms of inhibition that involve potentially synergistic ligand combinations. AMP alone adopts the productive binding mode of IMP and yet stabilizes the active site in a conformation that favors the binding of Mg(2+)-IMP to the GTP pocket. On the other hand, AMP, in the presence of GDP, orthophosphate, and Mg(2+), adopts the binding mode of adenylosuccinate. Depending on circumstances then, AMP behaves as an analogue of IMP or as an analogue of adenylosuccinate. The complex of adenylosuccinate.GDP.Mg(2+).sulfate, the first structure of an adenylosuccinate-bound synthetase, reveals significant geometric distortions and tight nonbonded contacts relevant to the proposed catalytic mechanism. Adenylosuccinate forms from 6-phosphoryl-IMP and l-aspartate by the movement of the purine ring into the alpha-amino group of l-aspartate. Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase.,Iancu CV, Borza T, Fromm HJ, Honzatko RB J Biol Chem. 2002 Oct 25;277(43):40536-43. Epub 2002 Aug 16. PMID:12186864 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adenylosuccinate synthetase 3D structures

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