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1tb4

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[[Image:1tb4.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus influenzae with a Bound Periodate==
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|PDB= 1tb4 |SIZE=350|CAPTION= <scene name='initialview01'>1tb4</scene>, resolution 2.15&Aring;
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<StructureSection load='1tb4' size='340' side='right'caption='[[1tb4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PEJ:PERIODATE'>PEJ</scene>
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<table><tr><td colspan='2'>[[1tb4]] 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=1TB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TB4 FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.15&#8491;</td></tr>
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|GENE= ASD, HI0646 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEJ:PERIODATE'>PEJ</scene></td></tr>
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}}
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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=1tb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tb4 OCA], [https://pdbe.org/1tb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tb4 RCSB], [https://www.ebi.ac.uk/pdbsum/1tb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tb4 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/tb/1tb4_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=1tb4 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 Periodate'''
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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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1TB4 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=1TB4 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]]
[[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: PEJ]]
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[[Category: aspartate biosynthetic pathway]]
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[[Category: aspartate-semialdehyde dehydrogenase]]
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[[Category: periodate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:16:09 2008''
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Current revision

Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus influenzae with a Bound Periodate

PDB ID 1tb4

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