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2e5v

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[[Image:2e5v.jpg|left|200px]]<br /><applet load="2e5v" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2e5v, resolution 2.09&Aring;" />
 
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'''Crystal structure of L-Aspartate Oxidase from hyperthermophilic archaeon Sulfolobus tokodaii'''<br />
 
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==Overview==
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==Crystal structure of L-Aspartate Oxidase from hyperthermophilic archaeon Sulfolobus tokodaii==
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The crystal structure of the highly thermostable l-aspartate oxidase (LAO) from the hyperthermophilic archaeon Sulfolobus tokodaii was determined at a 2.09 A resolution. The factors contributing to the thermostability of the enzyme were analyzed by comparing its structure to that of Escherichia coli LAO. Like E. coli LAO, the S. tokodaii enzyme consists of three domains: an FAD-binding domain, an alpha+beta capping domain, and a C-terminal three-helix bundle. However, the situation of the linker between the FAD-binding domain and C-terminal three-helix bundle in S. tokodaii LAO is completely different from that in E. coli LAO, where the linker is situated near the FAD-binding domain and has virtually no interaction with the rest of the protein. In S. tokodaii LAO, this linker is situated near the C-terminal three-helix bundle and contains a beta-strand that runs parallel to the C-terminal strand. This results in the formation of an additional beta-sheet, which appears to reduce the flexibility of the C-terminal region. Furthermore, the displacement of the linker enables formation of a 5-residue ion-pair network between the FAD-binding and C-terminal domains, which strengthens the interdomain interactions. These features might be the main factors contributing to the high thermostability of S. tokodaii LAO.
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<StructureSection load='2e5v' size='340' side='right'caption='[[2e5v]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2e5v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii Sulfurisphaera tokodaii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E5V FirstGlance]. <br>
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2E5V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-aspartate_oxidase L-aspartate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.16 1.4.3.16] Known structural/functional Sites: <scene name='pdbsite=AC1:Cl+Binding+Site+For+Residue+A+2001'>AC1</scene>, <scene name='pdbsite=AC2:Cl+Binding+Site+For+Residue+B+2002'>AC2</scene>, <scene name='pdbsite=AC3:Fad+Binding+Site+For+Residue+B+1001'>AC3</scene> and <scene name='pdbsite=AC4:Fad+Binding+Site+For+Residue+A+1002'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5V OCA].
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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]] 2.09&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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==Reference==
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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=2e5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5v OCA], [https://pdbe.org/2e5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e5v RCSB], [https://www.ebi.ac.uk/pdbsum/2e5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5v ProSAT]</span></td></tr>
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Structure of l-aspartate oxidase from the hyperthermophilic archaeon Sulfolobus tokodaii., Sakuraba H, Yoneda K, Asai I, Tsuge H, Katunuma N, Ohshima T, Biochim Biophys Acta. 2008 Mar;1784(3):563-71. Epub 2008 Jan 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18226609 18226609]
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</table>
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[[Category: L-aspartate oxidase]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/NADB_SULTO NADB_SULTO] Catalyzes the oxidation of L-aspartate to iminoaspartate.
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[[Category: Sulfolobus tokodaii]]
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== Evolutionary Conservation ==
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[[Category: Asai, I.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Katunuma, N.]]
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Check<jmol>
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[[Category: Ohshima, T.]]
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<jmolCheckbox>
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[[Category: Sakuraba, H.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/2e5v_consurf.spt"</scriptWhenChecked>
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[[Category: Tsuge, H.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Yoneda, K.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: CL]]
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</jmolCheckbox>
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[[Category: FAD]]
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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=2e5v ConSurf].
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[[Category: archaea]]
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<div style="clear:both"></div>
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[[Category: l-aspartate oxidase]]
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__TOC__
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[[Category: oxidoreductase]]
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</StructureSection>
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[[Category: Large Structures]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 5 13:25:20 2008''
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[[Category: Sulfurisphaera tokodaii]]
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[[Category: Asai I]]
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[[Category: Katunuma N]]
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[[Category: Ohshima T]]
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[[Category: Sakuraba H]]
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[[Category: Tsuge H]]
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[[Category: Yoneda K]]

Current revision

Crystal structure of L-Aspartate Oxidase from hyperthermophilic archaeon Sulfolobus tokodaii

PDB ID 2e5v

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