7yq0

Crystal structure of adenosine 5'-phosphosulfate kinase from Archaeoglobus fulgidus in complex with ADP

spinqualitylabelsall models 7yq0, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7yq0 is a 2 chain structure with sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.58Å Ligands: ADP, GOL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A101DF63_ARCFL Catalyzes the synthesis of activated sulfate.[HAMAP-Rule:MF_00065][RuleBase:RU004347] Publication Abstract from PubMed The 3'-phosphoadenosine-5'-phosphosulfate (PAPS) molecule is essential during enzyme-catalyzed sulfation reactions as a sulfate donor and is an intermediate in the reduction of sulfate to sulfite in the sulfur assimilation pathway. PAPS is produced through a two-step reaction involving ATP sulfurylase and adenosine 5'-phosphosulfate (APS) kinase enzymes/domains. However, archaeal APS kinases have not yet been characterized and their mechanism of action remains unclear. Here, we first structurally characterized APS kinase from the hyperthermophilic archaeon Archaeoglobus fulgidus, (AfAPSK). We demonstrated the PAPS production activity of AfAPSK at the optimal growth temperature (83 degrees C). Furthermore, we determined the two crystal structures of AfAPSK: ADP complex and ATP analog adenylyl-imidodiphosphate (AMP-PNP)/Mg(2+)/APS complex. Structural and complementary mutational analyses revealed the catalytic and substrate recognition mechanisms of AfAPSK. This study also hints at the molecular basis behind the thermal stability of AfAPSK. Crystal structure of adenosine 5'-phosphosulfate kinase isolated from Archaeoglobus fulgidus.,Kawakami T, Teramoto T, Kakuta Y Biochem Biophys Res Commun. 2022 Dec 29;643:105-110. doi: , 10.1016/j.bbrc.2022.12.081. PMID:36592583 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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