|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.== | | ==1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.== |
| - | <StructureSection load='1t4b' size='340' side='right' caption='[[1t4b]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='1t4b' size='340' side='right'caption='[[1t4b]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1t4b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T4B FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t4d|1t4d]]</td></tr>
| + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASD, HOM, B3433, Z4797, ECS4278, SF3456, S4307 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | <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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4b OCA], [http://pdbe.org/1t4b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t4b RCSB], [http://www.ebi.ac.uk/pdbsum/1t4b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t4b ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 33: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Aspartate-semialdehyde dehydrogenase|Aspartate-semialdehyde dehydrogenase]] | + | *[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Aspartate-semialdehyde dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Dhaliwal, B]] | + | [[Category: Dhaliwal B]] |
| - | [[Category: Hawkins, A R]] | + | [[Category: Hawkins AR]] |
| - | [[Category: Lockyer, M]] | + | [[Category: Lockyer M]] |
| - | [[Category: Nichols, C E]] | + | [[Category: Nichols CE]] |
| - | [[Category: Stammers, D K]] | + | [[Category: Stammers DK]] |
| - | [[Category: Asadh]]
| + | |
| - | [[Category: Aspartate semialdehyde dehydrogenase]]
| + | |
| - | [[Category: Domain movement]]
| + | |
| - | [[Category: Hosr]]
| + | |
| - | [[Category: Lysine biosynthesis]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
DHAS_ECOLI Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Biellmann JF, Eid P, Hirth C, Jornvall H. Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Purification and general properties. Eur J Biochem. 1980 Feb;104(1):53-8. PMID:6102909
- ↑ Chassagnole C, Rais B, Quentin E, Fell DA, Mazat JP. An integrated study of threonine-pathway enzyme kinetics in Escherichia coli. Biochem J. 2001 Jun 1;356(Pt 2):415-23. PMID:11368768
- ↑ Nichols CE, Dhaliwal B, Lockyer M, Hawkins AR, Stammers DK. High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase. J Mol Biol. 2004 Aug 13;341(3):797-806. PMID:15288787 doi:http://dx.doi.org/10.1016/j.jmb.2004.05.073
|
