1M8P

Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state

Summary for 1M8P

• Entry DOI: 10.2210/pdb1m8p/pdb
• Related: 1G8G 1I2D 1JHD
• Descriptor: sulfate adenylyltransferase, 3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE (3 entities in total)
• Functional Keywords: rossmann fold, phosphosulfate binding, t-state, transferase
• Biological source: Penicillium chrysogenum
• Cellular location: Cytoplasm (By similarity): Q12650
• Total number of polymer chains: 3
• Total formula weight: 193709.27

Authors

MacRae, I.J.,Segel, I.H.,Fisher, A.J. (deposition date: 2002-07-25, release date: 2002-11-27, Last modification date: 2024-02-14)

Primary citation

MacRae, I.J.,Segel, I.H.,Fisher, A.J.
Allosteric Inhibition via R-State Destabilization in ATP Sulfurylase from Penicillium chrysogenum
Nat.Struct.Biol., 9:945-949, 2002

PubMed Abstract: The structure of the cooperative hexameric enzyme ATP sulfurylase from Penicillium chrysogenum bound to its allosteric inhibitor, 3'-phosphoadenosine-5'-phosphosulfate (PAPS), was determined to 2.6 A resolution. This structure represents the low substrate-affinity T-state conformation of the enzyme. Comparison with the high substrate-affinity R-state structure reveals that a large rotational rearrangement of domains occurs as a result of the R-to-T transition. The rearrangement is accompanied by the 17 A movement of a 10-residue loop out of the active site region, resulting in an open, product release-like structure of the catalytic domain. Binding of PAPS is proposed to induce the allosteric transition by destabilizing an R-state-specific salt linkage between Asp 111 in an N-terminal domain of one subunit and Arg 515 in the allosteric domain of a trans-triad subunit. Disrupting this salt linkage by site-directed mutagenesis induces cooperative inhibition behavior in the absence of an allosteric effector, confirming the role of these two residues.

PubMed: 12426581
DOI: 10.1038/nsb868

Experimental method

X-RAY DIFFRACTION (2.6 Å)