1ta4

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[[Image:1ta4.gif|left|200px]]
 
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==Crystal Structure Of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with a Bound Arsenate==
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The line below this paragraph, containing "STRUCTURE_1ta4", creates the "Structure Box" on the page.
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<StructureSection load='1ta4' size='340' side='right'caption='[[1ta4]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1ta4| PDB=1ta4 | SCENE= }}
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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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'''Crystal Structure Of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with a Bound Arsenate'''
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==See Also==
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*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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1TA4 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/15583380 15583380]
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[[Category: Aspartate-semialdehyde dehydrogenase]]
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[[Category: Haemophilus influenzae]]
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[[Category: Single protein]]
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[[Category: Viola, R E.]]
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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]]
[[Category: Haemophilus influenzae]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:43:46 2008''
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[[Category: Large Structures]]
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[[Category: Viola RE]]

Current revision

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

PDB ID 1ta4

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