4maf: Difference between revisions
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<StructureSection load='4maf' size='340' side='right' caption='[[4maf]], [[Resolution|resolution]] 2.48Å' scene=''> | <StructureSection load='4maf' size='340' side='right' caption='[[4maf]], [[Resolution|resolution]] 2.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
[[4maf]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAF OCA]. <br> | <table><tr><td colspan='2'>[[4maf]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAF OCA]. <br> | ||
<b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene><br> | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene><br> | ||
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | ||
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4maf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4maf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4maf RCSB], [http://www.ebi.ac.uk/pdbsum/4maf PDBsum]</span>< | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4maf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4maf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4maf RCSB], [http://www.ebi.ac.uk/pdbsum/4maf PDBsum]</span></td></tr> | ||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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 (GmATPS) 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 to other ATP sulfurylases, but similar to mammalian PAPS synthetase. Steady-state kinetic analysis of twenty GmATPS point mutants suggests a reaction mechanism in which nucleophilic attack by sulfate on the alpha-phosphate of ATP involves transition state stabilization by Arg248, Asn249, His255, and Arg349. 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. | 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 (GmATPS) 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 to other ATP sulfurylases, but similar to mammalian PAPS synthetase. Steady-state kinetic analysis of twenty GmATPS point mutants suggests a reaction mechanism in which nucleophilic attack by sulfate on the alpha-phosphate of ATP involves transition state stabilization by Arg248, Asn249, His255, and Arg349. 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. | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:40, 1 May 2014
Soybean ATP SulfurylaseSoybean ATP Sulfurylase
Structural highlights
Publication Abstract from PubMedEnzymes 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 (GmATPS) 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 to other ATP sulfurylases, but similar to mammalian PAPS synthetase. Steady-state kinetic analysis of twenty GmATPS point mutants suggests a reaction mechanism in which nucleophilic attack by sulfate on the alpha-phosphate of ATP involves transition state stabilization by Arg248, Asn249, His255, and Arg349. 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. Structure and Mechanism of Soybean ATP Sulfurylase and the Committed Step in Plant Sulfur Assimilation.,Herrmann J, Ravilious GE, McKinney SE, Westfall CS, Lee SG, Baraniecka P, Giovannetti M, Kopriva S, Krishnan HB, Jez JM J Biol Chem. 2014 Feb 28. PMID:24584934[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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