The Crystal Structure of Human PAPS Synthetase 1 Reveals Asymmetry in Substrate Binding

The high energy sulfate donor 3′-phosphoadenosine-5-phosphosulfate (PAPS) is used for sulfate conjugation of extracellular matrix, hormones and drugs. Human PAPS synthetase 1 catalyzes two subsequent reactions starting from ATP and sulfate. First the ATP sulfurylase domain forms APS, then the APS ki...

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Veröffentlicht in:	Journal of molecular biology 2005-04, Vol.347 (3), p.623-635
Hauptverfasser:	Harjes, Stefan, Bayer, Peter, Scheidig, Axel J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Diphosphate - metabolism adenosine phosphosulfate Amino Acid Sequence asymmetric homodimer Binding Sites Coenzymes - metabolism Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Molecular Structure Multienzyme Complexes - chemistry Multienzyme Complexes - metabolism P-loop phosphoadenosine phosphosulfate Protein Binding Protein Structure, Tertiary Sequence Alignment Sulfate Adenylyltransferase - chemistry Sulfate Adenylyltransferase - metabolism
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