1t4b

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[[Image:1t4b.jpg|left|200px]]
 
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{{Structure
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==1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.==
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|PDB= 1t4b |SIZE=350|CAPTION= <scene name='initialview01'>1t4b</scene>, resolution 1.60&Aring;
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<StructureSection load='1t4b' size='340' side='right'caption='[[1t4b]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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<table><tr><td colspan='2'>[[1t4b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T4B 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]] 1.6&#8491;</td></tr>
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|GENE= ASD, HOM, B3433, Z4797, ECS4278, SF3456, S4307 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=1t4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4b OCA], [https://pdbe.org/1t4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t4b RCSB], [https://www.ebi.ac.uk/pdbsum/1t4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t4b ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHAS_ECOLI DHAS_ECOLI] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.<ref>PMID:6102909</ref> <ref>PMID:11368768</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/t4/1t4b_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=1t4b ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Two high-resolution structures have been determined for Eschericia coli aspartate beta-semialdehyde dehydrogenase (ecASADH), an enzyme of the aspartate biosynthetic pathway, which is a potential target for novel antimicrobial drugs. Both ASADH structures were of the open form and were refined to 1.95 A and 1.6 A resolution, allowing a more detailed comparison with the closed form of the enzyme than previously possible. A more complex scheme for domain closure is apparent with the subunit being split into two further sub-domains with relative motions about three hinge axes. Analysis of hinge data and torsion-angle difference plots is combined to allow the proposal of a detailed structural mechanism for ecASADH domain closure. Additionally, asymmetric distortions of individual subunits are identified, which form the basis for the previously reported "half-of-the-sites reactivity" (HOSR). A putative explanation of this arrangement is also presented, suggesting the HOSR system may provide a means for ecASADH to offset the energy required to remobilise flexible loops at the end of the reaction cycle, and hence avoid falling into an energy minimum.
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'''1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.'''
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High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase.,Nichols CE, Dhaliwal B, Lockyer M, Hawkins AR, Stammers DK J Mol Biol. 2004 Aug 13;341(3):797-806. PMID:15288787<ref>PMID:15288787</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1t4b" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Two high-resolution structures have been determined for Eschericia coli aspartate beta-semialdehyde dehydrogenase (ecASADH), an enzyme of the aspartate biosynthetic pathway, which is a potential target for novel antimicrobial drugs. Both ASADH structures were of the open form and were refined to 1.95 A and 1.6 A resolution, allowing a more detailed comparison with the closed form of the enzyme than previously possible. A more complex scheme for domain closure is apparent with the subunit being split into two further sub-domains with relative motions about three hinge axes. Analysis of hinge data and torsion-angle difference plots is combined to allow the proposal of a detailed structural mechanism for ecASADH domain closure. Additionally, asymmetric distortions of individual subunits are identified, which form the basis for the previously reported "half-of-the-sites reactivity" (HOSR). A putative explanation of this arrangement is also presented, suggesting the HOSR system may provide a means for ecASADH to offset the energy required to remobilise flexible loops at the end of the reaction cycle, and hence avoid falling into an energy minimum.
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*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1T4B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4B OCA].
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__TOC__
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</StructureSection>
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==Reference==
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High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase., Nichols CE, Dhaliwal B, Lockyer M, Hawkins AR, Stammers DK, J Mol Biol. 2004 Aug 13;341(3):797-806. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15288787 15288787]
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[[Category: Aspartate-semialdehyde dehydrogenase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dhaliwal, B.]]
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[[Category: Dhaliwal B]]
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[[Category: Hawkins, A R.]]
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[[Category: Hawkins AR]]
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[[Category: Lockyer, M.]]
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[[Category: Lockyer M]]
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[[Category: Nichols, C E.]]
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[[Category: Nichols CE]]
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[[Category: Stammers, D K.]]
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[[Category: Stammers DK]]
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[[Category: NA]]
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[[Category: asadh]]
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[[Category: aspartate semialdehyde dehydrogenase]]
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[[Category: domain movement]]
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[[Category: hosr]]
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[[Category: lysine biosynthesis]]
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[[Category: nadp+ oxidoreductase (phosphorylating)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:13:36 2008''
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Current revision

1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.

PDB ID 1t4b

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