Motion in ATP Sulfurylase [atpsulf]

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Classification [D-h-2]

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 functionsulfate adenylyltransferase (ATP) activity, ATP binding, kinase activity, transferase activity, transferring phosphorus-containing groups
Biological processsulfate assimilation

Morphs

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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
245895-8891 ATP sulfurylase 1i2d [ A ] 1m8p [ A ] 573


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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu