PDBsum entry 1sur

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protein links
Oxidoreductase PDB id
Protein chain
215 a.a. *
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Phospho-adenylyl-sulfate reductase
Structure: Paps reductase. Chain: a. Synonym: phosphoadenosine phosphosulfate reductase. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Strain: jm96. Atcc: genetic stock center, strain cgsc 5746. Collection: genetic stock center, strain cgsc 5746. Cellular_location: cytoplasm. Gene: cysh
Biol. unit: Dimer (from PDB file)
2.00Å     R-factor:   0.190     R-free:   0.230
Authors: I.Sinning,H.Savage
Key ref:
H.Savage et al. (1997). Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Structure, 5, 895-906. PubMed id: 9261082 DOI: 10.1016/S0969-2126(97)00244-X
01-Apr-98     Release date:   11-May-99    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P17854  (CYSH_ECOLI) -  Phosphoadenosine phosphosulfate reductase
244 a.a.
215 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Phosphoadenylyl-sulfate reductase (thioredoxin).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
Adenosine 3',5'-bisphosphate
+ sulfite
+ thioredoxin disulfide
= 3'-phosphoadenylyl sulfate
+ thioredoxin
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     2 terms  


DOI no: 10.1016/S0969-2126(97)00244-X Structure 5:895-906 (1997)
PubMed id: 9261082  
Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.
H.Savage, G.Montoya, C.Svensson, J.D.Schwenn, I.Sinning.
BACKGROUND: Assimilatory sulphate reduction supplies prototrophic organisms with reduced sulphur for the biosynthesis of all sulphur-containing metabolites. This process is driven by a sequence of enzymatic steps involving phosphoadenylyl sulphate (PAPS) reductase. Thioredoxin is used as the electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP) and sulphite. Unlike most electron-transfer reactions, there are no cofactors or prosthetic groups involved in this reduction and PAPS reductase is one of the rare examples of an enzyme that is able to store two electrons. Determination of the structure of PAPS reductase is the first step towards elucidating the biochemical details of the reduction of PAPS to sulphite. RESULTS: We have determined the crystal structure of PAPS reductase at 2.0 A resolution in the open, reduced form, in which a flexible loop covers the active site. The protein is active as a dimer, each monomer consisting of a central six-stranded beta sheet with alpha helices packing against each side. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. CONCLUSIONS: The sequence conservation between ATP sulphurylases, a subfamily of ATP PPases, and PAPS reductase and the similarities in both their mechanisms and folds, suggest an evolutionary link between the ATP PPases and PAPS reductases. Together with the N type ATP PPases, PAPS reductases and ATP sulphurylases are proposed to form a new family of homologous enzymes with adenine nucleotide alpha-hydrolase activity. The open, reduced form of PAPS reductase is able to bind PAPS, whereas the closed oxidized form cannot. A movement between the two monomers of the dimer may allow this switch in conformation to occur.
  Selected figure(s)  
Figure 1.
Figure 1. The reaction catalyzed by PAPS reductase: phosphoadenylyl sulphate (PAPS) is reduced to phospho-adenosine-phosphate (PAP) and sulphite.
  The above figure is reprinted by permission from Cell Press: Structure (1997, 5, 895-906) copyright 1997.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19375431 C.Huerta, D.Borek, M.Machius, N.V.Grishin, and H.Zhang (2009).
Structure and mechanism of a eukaryotic FMN adenylyltransferase.
  J Mol Biol, 389, 388-400.
PDB codes: 3fwk 3g59 3g5a 3g6k
19678707 J.A.Hong, D.P.Bhave, and K.S.Carroll (2009).
Identification of critical ligand binding determinants in Mycobacterium tuberculosis adenosine-5'-phosphosulfate reductase.
  J Med Chem, 52, 5485-5495.  
19744922 J.S.Chung, V.Noguera-Mazon, J.M.Lancelin, S.K.Kim, M.Hirasawa, M.Hologne, T.Leustek, and D.B.Knaff (2009).
Interaction domain on thioredoxin for Pseudomonas aeruginosa 5'-adenylylsulfate reductase.
  J Biol Chem, 284, 31181-31189.  
19067028 M.E.Bradley, J.S.Rest, W.H.Li, and N.B.Schwartz (2009).
Sulfate activation enzymes: phylogeny and association with pyrophosphatase.
  J Mol Evol, 68, 1.  
17803682 I.Pérez-Arellano, J.Gallego, and J.Cervera (2007).
The PUA domain - a structural and functional overview.
  FEBS J, 274, 4972-4984.  
17890313 I.Vallet-Gely, J.S.Sharp, and S.L.Dove (2007).
Local and global regulators linking anaerobiosis to cupA fimbrial gene expression in Pseudomonas aeruginosa.
  J Bacteriol, 189, 8667-8676.  
17519237 S.Kopriva, K.Fritzemeier, G.Wiedemann, and R.Reski (2007).
The putative moss 3'-phosphoadenosine-5'-phosphosulfate reductase is a novel form of adenosine-5'-phosphosulfate reductase without an iron-sulfur cluster.
  J Biol Chem, 282, 22930-22938.  
17010373 J.Chartron, K.S.Carroll, C.Shiau, H.Gao, J.A.Leary, C.R.Bertozzi, and C.D.Stout (2006).
Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5'-phosphosulfate reductase.
  J Mol Biol, 364, 152-169.
PDB code: 2goy
16387658 J.D.Mougous, D.H.Lee, S.C.Hubbard, M.W.Schelle, D.J.Vocadlo, J.M.Berger, and C.R.Bertozzi (2006).
Molecular basis for G protein control of the prokaryotic ATP sulfurylase.
  Mol Cell, 21, 109-122.
PDB code: 1zun
14627706 C.Berndt, C.H.Lillig, M.Wollenberg, E.Bill, M.C.Mansilla, Mendoza, A.Seidler, and J.D.Schwenn (2004).
Characterization and reconstitution of a 4Fe-4S adenylyl sulfate/phosphoadenylyl sulfate reductase from Bacillus subtilis.
  J Biol Chem, 279, 7850-7855.  
12682041 C.H.Lillig, A.Potamitou, J.D.Schwenn, A.Vlamis-Gardikas, and A.Holmgren (2003).
Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins.
  J Biol Chem, 278, 22325-22330.  
14506286 D.E.Pilloff, and T.S.Leyh (2003).
Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system.
  J Biol Chem, 278, 50435-50441.  
12144918 J.D.Mougous, R.E.Green, S.J.Williams, S.E.Brenner, and C.R.Bertozzi (2002).
Sulfotransferases and sulfatases in mycobacteria.
  Chem Biol, 9, 767-776.  
10613872 J.A.Bick, J.J.Dennis, G.J.Zylstra, J.Nowack, and T.Leustek (2000).
Identification of a new class of 5'-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria.
  J Bacteriol, 182, 135-142.  
10625629 M.Suter, P.von Ballmoos, S.Kopriva, R.O.den Camp, J.Schaller, C.Kuhlemeier, P.Schürmann, and C.Brunold (2000).
Adenosine 5'-phosphosulfate sulfotransferase and adenosine 5'-phosphosulfate reductase are identical enzymes.
  J Biol Chem, 275, 930-936.  
10075658 C.H.Lillig, A.Prior, J.D.Schwenn, F.Aslund, D.Ritz, A.Vlamis-Gardikas, and A.Holmgren (1999).
New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase.
  J Biol Chem, 274, 7695-7698.  
9666334 L.Holm (1998).
Unification of protein families.
  Curr Opin Struct Biol, 8, 372-379.  
9753692 M.Rizzi, M.Bolognesi, and A.Coda (1998).
A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure.
  Structure, 6, 1129-1140.
PDB code: 2nsy
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.