1m8p
From Proteopedia
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|PDB= 1m8p |SIZE=350|CAPTION= <scene name='initialview01'>1m8p</scene>, resolution 2.60Å | |PDB= 1m8p |SIZE=350|CAPTION= <scene name='initialview01'>1m8p</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PPS:3 | + | |LIGAND= <scene name='pdbligand=PPS:3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE'>PPS</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] | |ACTIVITY= [http://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] | ||
|GENE= | |GENE= | ||
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[[Category: t-state]] | [[Category: t-state]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:43:53 2008'' |
Revision as of 10:43, 23 March 2008
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| , resolution 2.60Å | |||||||
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| Ligands: | |||||||
| Activity: | Sulfate adenylyltransferase, with EC number 2.7.7.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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