1m8p

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[[Image:1m8p.gif|left|200px]]
[[Image:1m8p.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1m8p |SIZE=350|CAPTION= <scene name='initialview01'>1m8p</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1m8p", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PPS:3&#39;-PHOSPHATE-ADENOSINE-5&#39;-PHOSPHATE+SULFATE'>PPS</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1m8p| PDB=1m8p | SCENE= }}
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|RELATEDENTRY=[[1i2d|1I2D]], [[1g8g|1G8G]], [[1jhd|1JHD]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m8p OCA], [http://www.ebi.ac.uk/pdbsum/1m8p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m8p RCSB]</span>
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}}
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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.]]
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[[Category: phosphosulfate binding]]
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[[Category: Phosphosulfate binding]]
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[[Category: rossmann fold]]
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[[Category: Rossmann fold]]
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[[Category: t-state]]
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[[Category: T-state]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:46:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:12:50 2008''
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Revision as of 21:46, 2 May 2008

Template:STRUCTURE 1m8p

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

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