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1dof

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[[Image:1dof.gif|left|200px]]
 
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{{Structure
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==THE CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE FROM PYROBACULUM AEROPHILUM: INSIGHTS INTO THERMAL STABILITY AND HUMAN PATHOLOGY==
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|PDB= 1dof |SIZE=350|CAPTION= <scene name='initialview01'>1dof</scene>, resolution 2.10&Aring;
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<StructureSection load='1dof' size='340' side='right'caption='[[1dof]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylosuccinate_lyase Adenylosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.2 4.3.2.2] </span>
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</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>
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|GENE=
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1c3c|1c3c]], [[1c3u|1c3u]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dof OCA], [http://www.ebi.ac.uk/pdbsum/1dof PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dof RCSB]</span>
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[https://www.uniprot.org/uniprot/Q8ZY28_PYRAE Q8ZY28_PYRAE]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/1dof_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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'''THE CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE FROM PYROBACULUM AEROPHILUM: INSIGHTS INTO THERMAL STABILITY AND HUMAN PATHOLOGY'''
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==See Also==
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*[[Adenylosuccinate lyase 3D structures|Adenylosuccinate lyase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1DOF is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10926519 10926519]
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[[Category: Adenylosuccinate lyase]]
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[[Category: Pyrobaculum aerophilum]]
[[Category: Pyrobaculum aerophilum]]
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[[Category: Single protein]]
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[[Category: Dixon JE]]
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[[Category: Dixon, J E.]]
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[[Category: Goedken E]]
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[[Category: Goedken, E.]]
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[[Category: Marqusee S]]
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[[Category: Marqusee, S.]]
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[[Category: Toth EA]]
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[[Category: Toth, E A.]]
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[[Category: Yeates TO]]
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[[Category: Yeates, T O.]]
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[[Category: lyase]]
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[[Category: purine biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:45:30 2008''
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Current revision

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

PDB ID 1dof

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