1m8p

<table><tr><td colspan='2'>[[1m8p]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10106 Atcc 10106]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M8P FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PPS:3-PHOSPHATE-ADENOSINE-5-PHOSPHATE+SULFATE'>PPS</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i2d|1i2d]], [[1g8g|1g8g]], [[1jhd|1jhd]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1m8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m8p RCSB], [http://www.ebi.ac.uk/pdbsum/1m8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m8p ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MET3_PENCH MET3_PENCH]] Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12426581</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1m8p" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 10106]]

[[Category: Sulfate adenylyltransferase]]

[[Category: Fisher, A J]]

[[Category: MacRae, I J]]

[[Category: Segel, I H]]

[[Category: Transferase]]