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1m8p
From Proteopedia
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[[Image:1m8p.gif|left|200px]] | [[Image:1m8p.gif|left|200px]] | ||
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'''Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state''' | '''Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state''' | ||
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[[Category: MacRae, I J.]] | [[Category: MacRae, I J.]] | ||
[[Category: Segel, I H.]] | [[Category: Segel, I H.]] | ||
| - | [[Category: | + | [[Category: Phosphosulfate binding]] |
| - | [[Category: | + | [[Category: Rossmann fold]] |
| - | [[Category: | + | [[Category: T-state]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:46:09 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:46, 2 May 2008
Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state
Overview
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.
About this Structure
1M8P is a Single protein structure of sequence from Penicillium chrysogenum. Full crystallographic information is available from OCA.
Reference
Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum., MacRae IJ, Segel IH, Fisher AJ, Nat Struct Biol. 2002 Dec;9(12):945-9. PMID:12426581 Page seeded by OCA on Sat May 3 00:46:09 2008
