1m8p

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(New page: 200px<br /><applet load="1m8p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m8p, resolution 2.60&Aring;" /> '''Crystal Structure of...)
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[[Image:1m8p.gif|left|200px]]<br /><applet load="1m8p" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1m8p.gif|left|200px]]<br /><applet load="1m8p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m8p, resolution 2.60&Aring;" />
caption="1m8p, resolution 2.60&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M8P OCA].
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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]]
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[[Category: Fisher, A.J.]]
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[[Category: Fisher, A J.]]
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[[Category: MacRae, I.J.]]
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[[Category: MacRae, I J.]]
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[[Category: Segel, I.H.]]
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[[Category: Segel, I H.]]
[[Category: PPS]]
[[Category: PPS]]
[[Category: phosphosulfate binding]]
[[Category: phosphosulfate binding]]
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[[Category: t-state]]
[[Category: t-state]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:14:04 2007''
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''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


1m8p, resolution 2.60Å

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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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