1m8p
From Proteopedia
(New page: 200px<br /><applet load="1m8p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m8p, resolution 2.60Å" /> '''Crystal Structure of...) |
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| - | [[Image:1m8p.gif|left|200px]]<br /><applet load="1m8p" size=" | + | [[Image:1m8p.gif|left|200px]]<br /><applet load="1m8p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m8p, resolution 2.60Å" /> | caption="1m8p, resolution 2.60Å" /> | ||
'''Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state'''<br /> | '''Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the cooperative hexameric enzyme ATP sulfurylase from | + | 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== | ==About this Structure== | ||
| - | 1M8P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum] with PPS as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1M8P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum] with <scene name='pdbligand=PPS:'>PPS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M8P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfate adenylyltransferase]] | [[Category: Sulfate adenylyltransferase]] | ||
| - | [[Category: Fisher, A | + | [[Category: Fisher, A J.]] |
| - | [[Category: MacRae, I | + | [[Category: MacRae, I J.]] |
| - | [[Category: Segel, I | + | [[Category: Segel, I H.]] |
[[Category: PPS]] | [[Category: PPS]] | ||
[[Category: phosphosulfate binding]] | [[Category: phosphosulfate binding]] | ||
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[[Category: t-state]] | [[Category: t-state]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:42 2008'' |
Revision as of 11:52, 21 February 2008
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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 with as ligand. Active as Sulfate adenylyltransferase, with EC number 2.7.7.4 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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