1m8p: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state'''<br />


==Overview==
==Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state==
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.
<StructureSection load='1m8p' size='340' side='right'caption='[[1m8p]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1m8p]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1M8P FirstGlance]. <br>
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].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PPS:3-PHOSPHATE-ADENOSINE-5-PHOSPHATE+SULFATE'>PPS</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m8p OCA], [https://pdbe.org/1m8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m8p RCSB], [https://www.ebi.ac.uk/pdbsum/1m8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m8p ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12426581 12426581]
</table>
== Function ==
[https://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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m8/1m8p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m8p ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Penicillium chrysogenum]]
[[Category: Penicillium chrysogenum]]
[[Category: Single protein]]
[[Category: Fisher AJ]]
[[Category: Sulfate adenylyltransferase]]
[[Category: MacRae IJ]]
[[Category: Fisher, A.J.]]
[[Category: Segel IH]]
[[Category: MacRae, I.J.]]
[[Category: Segel, I.H.]]
[[Category: PPS]]
[[Category: phosphosulfate binding]]
[[Category: rossmann fold]]
[[Category: t-state]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:14:04 2007''

Latest revision as of 10:41, 14 February 2024

Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-stateCrystal Structure of P. chrysogenum ATP Sulfurylase in the T-state

Structural highlights

1m8p is a 3 chain structure with sequence from Penicillium chrysogenum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1m8p, resolution 2.60Å

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