Motion in ATP Sulfurylase [atpsulf]
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Structures 1I2D 1M8P
Description ATP sulfurylase uses ATP hydrolysis to form sulfated AMP (APS) from inorganic sulfate. APS is then phosphorylated by another enzyme to form PAPS, which in Penicillum allosterically inhibits ATP sulfurylase. The enzyme is a hexamer composed of two three-subunit rings, each of which moves identically. The allosteric C-terminal domain rotates several degrees relative to the catalytic and N-terminal domains. The simple domain motion of each subunit results in a larger ring in the (inactive) T-state. A separate loop motion of 17 angstroms opens up the active site.
References I J MacRae, I H Segel, A J Fisher (2001). Crystal structure of ATP sulfurylase from Penicillium chrysogenum: insights into the allosteric regulation of sulfate assimilation. Biochemistry, 40:6795-804 [Medline info for 11389593] MacRae IJ, Segel IH, Fisher AJ (2002). Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum. Nat Struct Biol. 9:945-9. [Medline info for 12426581]
Data and Graphics Custom movie One half of the hexamer, showing the allosteric interactions. Custom movie Same as above, but with molecular surface rendered.
GO terms associated with structures Molecular function sulfate adenylyltransferase (ATP) activity, ATP binding, kinase activity, transferase activity, transferring phosphorus-containing groups Biological process sulfate assimilation
Morphs[ show all images ]
Best representative Morph Morph name Structure #1 Structure #2 Residues ATP sulfurylase 1i2d [ ] 1m8p [ ] 3432
User-submitted morphs Morph Morph name Structure #1 Structure #2 Residues ATP sulfurylase 1i2d [ A ] 1m8p [ A ] 573
Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu