6c85

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

spinqualitylabelsall models 6c85, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6c85 is a 2 chain structure with sequence from Blastomyces gilchristii SLH14081. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: PLQ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C5GC63_AJEDR 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate-semialdehyde dehydrogenase 3D structures

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