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1ta4

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(New page: 200px<br /><applet load="1ta4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ta4, resolution 2.28&Aring;" /> '''Crystal Structure Of...)
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[[Image:1ta4.gif|left|200px]]<br /><applet load="1ta4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ta4, resolution 2.28&Aring;" />
 
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'''Crystal Structure Of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with a Bound Arsenate'''<br />
 
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==Overview==
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==Crystal Structure Of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with a Bound Arsenate==
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The reversible dephosphorylation of beta-aspartyl phosphate to, L-aspartate-beta-semialdehyde (ASA) in the aspartate biosynthetic pathway, is catalyzed by aspartate-beta-semialdehyde dehydrogenase (ASADH). The, phosphate that is present to activate the aspartate carboxyl group is held, in a separate and distinct binding site once removed and prior to its, release from the enzyme. This site had been shown to be selective for, tetrahedral oxyanions, with several competitive inhibitors and alternative, substrates previously identified for the reverse reaction. Structural, studies have now shown that the most potent oxyanion inhibitor (periodate), and a good alternative substrate (arsenate) each occupy the same catalytic, phosphate-binding site. However, a rotation of a threonine side chain, (Thr137) in the periodate complex disrupts an important hydrogen-bonding, interaction with an active-site glutamate (Glu243) that participates in, substrate orientation. This subtle change appears to be the difference, between a substrate and an inhibitor of this enzyme.
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<StructureSection load='1ta4' size='340' side='right'caption='[[1ta4]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ta4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TA4 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]] 2.28&#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=ART:ARSENATE'>ART</scene></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=1ta4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ta4 OCA], [https://pdbe.org/1ta4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ta4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ta4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ta4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHAS_HAEIN DHAS_HAEIN] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.<ref>PMID:12071715</ref>
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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/ta/1ta4_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=1ta4 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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1TA4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with ART as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TA4 OCA].
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*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-beta-semialdehyde dehydrogenase., Faehnle CR, Blanco J, Viola RE, Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2320-4. Epub, 2004 Nov 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15583380 15583380]
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__TOC__
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[[Category: Aspartate-semialdehyde dehydrogenase]]
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</StructureSection>
[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Viola, R.E.]]
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[[Category: Viola RE]]
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[[Category: ART]]
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[[Category: arsenate]]
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[[Category: aspartate biosynthetic pathway]]
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[[Category: aspartate-semialdehyde dehydrogenase]]
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[[Category: haemophilus influenzae]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:06:49 2007''
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Current revision

Crystal Structure Of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with a Bound Arsenate

PDB ID 1ta4

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