6c85
From Proteopedia
(Difference between revisions)
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==Crystal structure of aspartate semialdehyde dehydrogenase from Blastomyces dermatitidis with p-benzoquinone== | ==Crystal structure of aspartate semialdehyde dehydrogenase from Blastomyces dermatitidis with p-benzoquinone== | ||
| - | <StructureSection load='6c85' size='340' side='right' caption='[[6c85]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='6c85' size='340' side='right'caption='[[6c85]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6c85]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ajellomyces_dermatitidis_slh#14081 Ajellomyces dermatitidis slh#14081]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C85 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6c85]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ajellomyces_dermatitidis_slh#14081 Ajellomyces dermatitidis slh#14081]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C85 FirstGlance]. <br> | ||
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<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=6c85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c85 OCA], [http://pdbe.org/6c85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c85 RCSB], [http://www.ebi.ac.uk/pdbsum/6c85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c85 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=6c85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c85 OCA], [http://pdbe.org/6c85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c85 RCSB], [http://www.ebi.ac.uk/pdbsum/6c85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c85 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The aspartate pathway, uniquely found in plants and microorganisms, offers novel potential targets for the development of new antimicrobial drugs. Aspartate semialdehyde dehydrogenase (ASADH) catalyzes production of a key intermediate at the first branch point in this pathway. Several fungal ASADH structures have been determined, but the prior crystallization conditions had precluded complex formation with enzyme inhibitors. The first inhibitor-bound and cofactor-bound structures of ASADH from the pathogenic fungi Blastomyces dermatitidis have now been determined, along with a structural and functional comparison to other ASADH family members. The structure of this new ASADH is similar to the other fungal orthologs, but with some critical differences in the orientation of some active site functional groups and in the subunit interface region. The presence of this bound inhibitor reveals the first details about inhibitor binding interactions, and the flexible orientation of its aromatic ring provides helpful insights into the design of potentially more potent and selective antifungal compounds. | ||
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| + | Structural insights into inhibitor binding to a fungal ortholog of aspartate semialdehyde dehydrogenase.,Dahal GP, Viola RE Biochem Biophys Res Commun. 2018 Sep 18;503(4):2848-2854. doi:, 10.1016/j.bbrc.2018.08.053. Epub 2018 Aug 11. PMID:30107909<ref>PMID:30107909</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6c85" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ajellomyces dermatitidis slh#14081]] | [[Category: Ajellomyces dermatitidis slh#14081]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Dahal, G P]] | [[Category: Dahal, G P]] | ||
[[Category: Viola, R E]] | [[Category: Viola, R E]] | ||
Revision as of 17:52, 11 December 2019
Crystal structure of aspartate semialdehyde dehydrogenase from Blastomyces dermatitidis with p-benzoquinone
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