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6C85

Crystal structure of aspartate semialdehyde dehydrogenase from Blastomyces dermatitidis with p-benzoquinone

Summary for 6C85
Entry DOI10.2210/pdb6c85/pdb
DescriptorAspartate-semialdehyde dehydrogenase, 1,4-benzoquinone (3 entities in total)
Functional Keywordsrossman fold, oxidoreductase, antifungal inhibitor complex
Biological sourceBlastomyces gilchristii (Blastomyces dermatitidis)
Total number of polymer chains2
Total formula weight80522.14
Authors
Dahal, G.P.,Viola, R.E. (deposition date: 2018-01-24, release date: 2019-01-30, Last modification date: 2023-10-04)
Primary citationDahal, G.P.,Viola, R.E.
Structural insights into inhibitor binding to a fungal ortholog of aspartate semialdehyde dehydrogenase.
Biochem.Biophys.Res.Commun., 503:2848-2854, 2018
Cited by
PubMed Abstract: 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.
PubMed: 30107909
DOI: 10.1016/j.bbrc.2018.08.053
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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数据于2025-07-16公开中

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