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| | <StructureSection load='3q1l' size='340' side='right'caption='[[3q1l]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3q1l' size='340' side='right'caption='[[3q1l]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3q1l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Strr6 Strr6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q1L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3q1l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q1L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHL:2-AMINO-ETHANETHIOL'>DHL</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pwk|3pwk]], [[3pws|3pws]], [[3pyl|3pyl]], [[3pyx|3pyx]], [[3pzb|3pzb]], [[3pzr|3pzr]], [[3q0e|3q0e]], [[3q11|3q11]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHL:2-AMINO-ETHANETHIOL'>DHL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">asd, CGSSpBS455_08742, spr0918 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=171101 STRR6])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3q1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q1l OCA], [https://pdbe.org/3q1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q1l RCSB], [https://www.ebi.ac.uk/pdbsum/3q1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q1l ProSAT]</span></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=3q1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q1l OCA], [https://pdbe.org/3q1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q1l RCSB], [https://www.ebi.ac.uk/pdbsum/3q1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q1l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q8DQ00_STRR6 Q8DQ00_STRR6]] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate (By similarity).[HAMAP-Rule:MF_02121]
| + | [https://www.uniprot.org/uniprot/Q8DQ00_STRR6 Q8DQ00_STRR6] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate (By similarity).[HAMAP-Rule:MF_02121] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspartate-semialdehyde dehydrogenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strr6]] | + | [[Category: Streptococcus pneumoniae R6]] |
| - | [[Category: Pavlovsky, A G]] | + | [[Category: Pavlovsky AG]] |
| - | [[Category: Viola, R E]] | + | [[Category: Viola RE]] |
| - | [[Category: Nadp]]
| + | |
| - | [[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
| + | |
| Structural highlights
Function
Q8DQ00_STRR6 Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate (By similarity).[HAMAP-Rule:MF_02121]
Publication Abstract from PubMed
The aspartate biosynthetic pathway provides essential metabolites for many important biological functions, including the production of four essential amino acids. As this critical pathway is only present in plants and microbes, any disruptions will be fatal to these organisms. An early pathway enzyme, l-aspartate-beta-semialdehyde dehydrogenase, produces a key intermediate at the first branch point of this pathway. Developing potent and selective inhibitors against several orthologs in the l-aspartate-beta-semialdehyde dehydrogenase family can serve as lead compounds for antibiotic development. Kinetic studies of two small molecule fragment libraries have identified inhibitors that show good selectivity against l-aspartate-beta-semialdehyde dehydrogenases from two different bacterial species, Streptococcus pneumoniae and Vibrio cholerae, despite the presence of an identical constellation of active site amino acids in this homologous enzyme family. Structural characterization of enzyme-inhibitor complexes have elucidated different modes of binding between these structurally related enzymes. This information provides the basis for a structure-guided approach to the development of more potent and more selective inhibitors.
Structural Characterization of Inhibitors with Selectivity against Members of a Homologous Enzyme Family.,Pavlovsky AG, Liu X, Faehnle CR, Potente N, Viola RE Chem Biol Drug Des. 2012 Jan;79(1):128-36. doi:, 10.1111/j.1747-0285.2011.01267.x. Epub 2011 Nov 28. PMID:22039970[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pavlovsky AG, Liu X, Faehnle CR, Potente N, Viola RE. Structural Characterization of Inhibitors with Selectivity against Members of a Homologous Enzyme Family. Chem Biol Drug Des. 2012 Jan;79(1):128-36. doi:, 10.1111/j.1747-0285.2011.01267.x. Epub 2011 Nov 28. PMID:22039970 doi:10.1111/j.1747-0285.2011.01267.x
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