6C85
Crystal structure of aspartate semialdehyde dehydrogenase from Blastomyces dermatitidis with p-benzoquinone
Summary for 6C85
Entry DOI | 10.2210/pdb6c85/pdb |
Descriptor | Aspartate-semialdehyde dehydrogenase, 1,4-benzoquinone (3 entities in total) |
Functional Keywords | rossman fold, oxidoreductase, antifungal inhibitor complex |
Biological source | Blastomyces gilchristii (Blastomyces dermatitidis) |
Total number of polymer chains | 2 |
Total formula weight | 80522.14 |
Authors | Dahal, G.P.,Viola, R.E. (deposition date: 2018-01-24, release date: 2019-01-30, Last modification date: 2023-10-04) |
Primary citation | Dahal, 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: 30107909DOI: 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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