1f1o

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[[Image:1f1o.jpg|left|200px]]<br /><applet load="1f1o" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1f1o, resolution 3.25&Aring;" />
 
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'''STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES'''<br />
 
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==Overview==
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==STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES==
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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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<StructureSection load='1f1o' size='340' side='right'caption='[[1f1o]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1f1o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F1O FirstGlance]. <br>
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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]] 3.25&#8491;</td></tr>
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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=1f1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1o OCA], [https://pdbe.org/1f1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f1o RCSB], [https://www.ebi.ac.uk/pdbsum/1f1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PUR8_BACSU PUR8_BACSU] Influences the affinity of glutamyl--tRNA ligase for its substrates and increases its thermostability.
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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/f1/1f1o_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=1f1o ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1F1O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1O OCA].
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*[[Adenylosuccinate lyase 3D structures|Adenylosuccinate lyase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10926519 10926519]
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[[Category: Adenylosuccinate lyase]]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Toth, E A.]]
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[[Category: Toth EA]]
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[[Category: Yeates, T.]]
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[[Category: Yeates T]]
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[[Category: purine biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:48 2008''
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Current revision

STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES

PDB ID 1f1o

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