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<StructureSection load='1dof' size='340' side='right'caption='[[1dof]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1dof' size='340' side='right'caption='[[1dof]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1dof]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_51768 Atcc 51768]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1dof]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOF FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c3c|1c3c]], [[1c3u|1c3u]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenylosuccinate_lyase Adenylosuccinate lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.2 4.3.2.2] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dof OCA], [https://pdbe.org/1dof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dof RCSB], [https://www.ebi.ac.uk/pdbsum/1dof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dof ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dof OCA], [https://pdbe.org/1dof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dof RCSB], [https://www.ebi.ac.uk/pdbsum/1dof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dof ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8ZY28_PYRAE Q8ZY28_PYRAE]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1dof ConSurf].
</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=1dof ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Adenylosuccinate lyase catalyzes two separate reactions in the de novo purine biosynthetic pathway. Through its dual action in this pathway, adenylosuccinate lyase plays an integral part in cellular replication and metabolism. Mutations in the human enzyme can result in severe neurological disorders, including mental retardation with autistic features. The crystal structure of adenylosuccinate lyase from the hyperthermophilic archaebacterium Pyrobaculum aerophilum has been determined to 2.1 A resolution. Although both the fold of the monomer and the architecture of the tetrameric assembly are similar to adenylosuccinate lyase from the thermophilic eubacterium Thermotoga maritima, the archaebacterial lyase contains unique features. Surprisingly, the structure of adenylosuccinate lyase from P. aerophilum reveals that this intracellular protein contains three disulfide bonds that contribute significantly to its stability against thermal and chemical denaturation. The observation of multiple disulfide bonds in the recombinant form of the enzyme suggests the need for further investigations into whether the intracellular environment of P. aerophilum, and possibly other hyperthermophiles, may be compatible with protein disulfide bond formation. In addition, the protein is shorter in P. aerophilum than it is in other organisms. This abbreviation results from an internal excision of a cluster of helices that may be involved in protein-protein interactions in other organisms and may relate to the observed clinical effects of human mutations in that region.
The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds.,Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO J Mol Biol. 2000 Aug 11;301(2):433-50. PMID:10926519<ref>PMID:10926519</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dof" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Adenylosuccinate lyase 3D structures|Adenylosuccinate lyase 3D structures]]
*[[Adenylosuccinate lyase 3D structures|Adenylosuccinate lyase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Adenylosuccinate lyase]]
[[Category: Atcc 51768]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dixon, J E]]
[[Category: Pyrobaculum aerophilum]]
[[Category: Goedken, E]]
[[Category: Dixon JE]]
[[Category: Marqusee, S]]
[[Category: Goedken E]]
[[Category: Toth, E A]]
[[Category: Marqusee S]]
[[Category: Yeates, T O]]
[[Category: Toth EA]]
[[Category: Lyase]]
[[Category: Yeates TO]]
[[Category: Purine biosynthesis]]

Latest revision as of 09:51, 20 March 2024

THE CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE FROM PYROBACULUM AEROPHILUM: INSIGHTS INTO THERMAL STABILITY AND HUMAN PATHOLOGY

1dof, resolution 2.10Å

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