4MAF

Soybean ATP Sulfurylase

Summary for 4MAF

• Entry DOI: 10.2210/pdb4maf/pdb
• Descriptor: ATP sulfurylase, ADENOSINE-5'-PHOSPHOSULFATE (3 entities in total)
• Functional Keywords: atp sulfurylase, sulfur metabolism, transferase
• Biological source: Glycine max (soybeans)
• Total number of polymer chains: 8
• Total formula weight: 368155.80

Authors

Herrmann, J.,Ravilious, G.E.,McKinney, S.E.,Westfall, C.S.,Lee, S.G.,Krishnan, H.B.,Jez, J.M. (deposition date: 2013-08-16, release date: 2014-03-12, Last modification date: 2023-09-20)

Primary citation

Herrmann, J.,Ravilious, G.E.,McKinney, S.E.,Westfall, C.S.,Lee, S.G.,Baraniecka, P.,Giovannetti, M.,Kopriva, S.,Krishnan, H.B.,Jez, J.M.
Structure and mechanism of soybean ATP sulfurylase and the committed step in plant sulfur assimilation.
J.Biol.Chem., 289:10919-10929, 2014

PubMed Abstract: Enzymes of the sulfur assimilation pathway are potential targets for improving nutrient content and environmental stress responses in plants. The committed step in this pathway is catalyzed by ATP sulfurylase, which synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP. To better understand the molecular basis of this energetically unfavorable reaction, the x-ray crystal structure of ATP sulfurylase isoform 1 from soybean (Glycine max ATP sulfurylase) in complex with APS was determined. This structure revealed several highly conserved substrate-binding motifs in the active site and a distinct dimerization interface compared with other ATP sulfurylases but was similar to mammalian 3'-phosphoadenosine 5'-phosphosulfate synthetase. Steady-state kinetic analysis of 20 G. max ATP sulfurylase point mutants suggests a reaction mechanism in which nucleophilic attack by sulfate on the α-phosphate of ATP involves transition state stabilization by Arg-248, Asn-249, His-255, and Arg-349. The structure and kinetic analysis suggest that ATP sulfurylase overcomes the energetic barrier of APS synthesis by distorting nucleotide structure and identifies critical residues for catalysis. Mutations that alter sulfate assimilation in Arabidopsis were mapped to the structure, which provides a molecular basis for understanding their effects on the sulfur assimilation pathway.

PubMed: 24584934
DOI: 10.1074/jbc.M113.540401

Experimental method

X-RAY DIFFRACTION (2.48 Å)