4i5v | pdb_00004i5v

Crystal structure of yeast Ap4A phosphorylase Apa2 in complex with Ap4A

spinqualitylabelsall models 4i5v, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4i5v is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.696Å Ligands: B4P Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function APA2_YEAST Sustains the catabolism of Np-4-N' nucleotides, rather than their synthesis. Publication Abstract from PubMed The homeostasis of intracellular diadenosine 5',5-P(1),P(4)-tetraphosphate (Ap4A) in the yeast Saccharomyces cerevisiae is maintained by two 60% sequence-identical paralogs of Ap4A phosphorylases (Apa1 and Apa2). Enzymatic assays show that, compared to Apa1, Apa2 has a relatively higher phosphorylase activity towards Ap3A (5',5-P(1),P(3)-tetraphosphate), Ap4A, and Ap5A (5',5-P(1),P(5)-tetraphosphate), and Ap4A is the favorable substrate for both enzymes. To decipher the catalytic insights, we determined the crystal structures of Apa2 in the apo-, AMP-, and Ap4A-complexed forms at 2.30, 2.80, and 2.70A resolution, respectively. Apa2 is an alpha/beta protein with a core domain of a twisted eight-stranded antiparallel beta-sheet flanked by several alpha-helices, similar to the galactose-1-phosphate uridylyltransferase (GalT) members of the histidine triad (HIT) superfamily. However, a unique auxiliary domain enables an individual Apa2 monomer to possess an intact substrate-binding cleft, which is distinct from previously reported dimeric GalT proteins. This cleft is perfectly complementary to the favorable substrate Ap4A, the AMP and ATP moieties of which are perpendicular to each other, leaving the alpha-phosphate group exposed at the sharp turn against the catalytic residue His161. Structural comparisons combined with site-directed mutagenesis and activity assays enable us to define the key residues for catalysis. Furthermore, multiple-sequence alignment reveals that Apa2 and homologs represent canonical Ap4A phosphorylases, which could be grouped as a unique branch in the GalT family. Structures of yeast Apa2 reveal catalytic insights into a canonical AP(4)A phosphorylase of the histidine triad superfamily.,Hou WT, Li WZ, Chen Y, Jiang YL, Zhou CZ J Mol Biol. 2013 Aug 9;425(15):2687-98. doi: 10.1016/j.jmb.2013.04.018. Epub 2013, Apr 26. PMID:23628156 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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