5jw6
From Proteopedia
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<StructureSection load='5jw6' size='340' side='right' caption='[[5jw6]], [[Resolution|resolution]] 2.39Å' scene=''> | <StructureSection load='5jw6' size='340' side='right' caption='[[5jw6]], [[Resolution|resolution]] 2.39Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5jw6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JW6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JW6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jw6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfu Aspfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JW6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JW6 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFUA_3G06830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330879 ASPFU])</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='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=5jw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jw6 OCA], [http://pdbe.org/5jw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jw6 RCSB], [http://www.ebi.ac.uk/pdbsum/5jw6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jw6 ProSAT]</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=5jw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jw6 OCA], [http://pdbe.org/5jw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jw6 RCSB], [http://www.ebi.ac.uk/pdbsum/5jw6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jw6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aspartate-semialdehyde dehydrogenase (ASADH) functions at a critical junction in the aspartate biosynthetic pathway and represents a validated target for antimicrobial drug design. This enzyme catalyzes the NADPH-dependent reductive dephosphorylation of beta-aspartyl phosphate to produce the key intermediate aspartate semialdehyde. The absence of this entire pathway in humans and other mammals will allow the selective targeting of pathogenic microorganisms for antimicrobial development. Here, the X-ray structure of a new form of ASADH from the pathogenic fungal species Aspergillus fumigatus has been determined. The overall structure of this enzyme is similar to those of its bacterial orthologs, but there are some critical differences both in biological assembly and in secondary-structural features that can potentially be exploited for the development of species-selective drugs with selective toxicity against infectious fungal organisms. | ||
| + | |||
| + | Structure of a fungal form of aspartate-semialdehyde dehydrogenase from Aspergillus fumigatus.,Dahal GP, Viola RE Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):36-44. doi:, 10.1107/S2053230X16020070. Epub 2017 Jan 1. PMID:28045392<ref>PMID:28045392</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5jw6" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aspartate-semialdehyde dehydrogenase|Aspartate-semialdehyde dehydrogenase]] | *[[Aspartate-semialdehyde dehydrogenase|Aspartate-semialdehyde dehydrogenase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aspartate-semialdehyde dehydrogenase]] | [[Category: Aspartate-semialdehyde dehydrogenase]] | ||
| + | [[Category: Aspfu]] | ||
[[Category: Dahal, G P]] | [[Category: Dahal, G P]] | ||
[[Category: Viola, R E]] | [[Category: Viola, R E]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 06:23, 18 April 2018
Cystal structure of aspartate semialdehyde dehydrogenase from Aspergillus fumigatus
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