3HSK
Crystal Structure of Aspartate Semialdehyde Dehydrogenase with NADP from Candida albicans
Summary for 3HSK
| Entry DOI | 10.2210/pdb3hsk/pdb |
| Descriptor | Aspartate-semialdehyde dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | aspartate semialdehyde dehydrogenase, candida albicans nadp complex, amino-acid biosynthesis, oxidoreductase |
| Biological source | Candida albicans (yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 82909.11 |
| Authors | Arachea, B.T.,Pavlovsky, A.,Liu, X.,Viola, R.E. (deposition date: 2009-06-10, release date: 2010-02-02, Last modification date: 2023-09-06) |
| Primary citation | Arachea, B.T.,Liu, X.,Pavlovsky, A.G.,Viola, R.E. Expansion of the aspartate beta-semialdehyde dehydrogenase family: the first structure of a fungal ortholog. Acta Crystallogr.,Sect.D, 66:205-212, 2010 Cited by PubMed Abstract: The enzyme aspartate semialdehyde dehydrogenase (ASADH) catalyzes a critical transformation that produces the first branch-point intermediate in an essential microbial amino-acid biosynthetic pathway. The first structure of an ASADH isolated from a fungal species (Candida albicans) has been determined as a complex with its pyridine nucleotide cofactor. This enzyme is a functional dimer, with a similar overall fold and domain organization to the structurally characterized bacterial ASADHs. However, there are differences in the secondary-structural elements and in cofactor binding that are likely to cause the lower catalytic efficiency of this fungal enzyme. Alterations in the dimer interface, through deletion of a helical subdomain and replacement of amino acids that participate in a hydrogen-bonding network, interrupt the intersubunit-communication channels required to support an alternating-site catalytic mechanism. The detailed functional information derived from this new structure will allow an assessment of ASADH as a possible target for antifungal drug development. PubMed: 20124701DOI: 10.1107/S0907444909052834 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
