Abstract
Succinic semialdehyde dehydrogenase (SSADH) plays a critical role in the metabolism of the inhibitory neurotransmitter γ-aminobutyric acid (GABA) and catalyzes the NAD(P) +-coupled oxidation of succinic semialdehyde (SSA) to succinic acid (SA). SSADH from Streptococcus pyogenes has been purified and crystallized as the apoenzyme and in a complex with NAD +. The crystals of native and NAD +-complexed SSADH diffracted to resolutions of 1.6 and 1.7 Å, respectively, using a synchrotron-radiation source. Both crystals belonged to the orthorhombic space group P2 12 12 1, with unit-cell parameters a = 93.3, b = 100.3, c = 105.1 Å for the native crystal and a = 93.3, b = 100.3, c = 105.0 Å for the complex crystal. Preliminary molecular replacement confirmed the presence of one dimer in both crystals, corresponding to a Matthews coefficient (V M) of 2.37 Å 3 Da -1 and a solvent content of 48.0%.
Original language | English |
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Pages (from-to) | 288-291 |
Number of pages | 4 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 68 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2012 Mar |
Keywords
- GabD
- NAD
- Streptococcus pyogenes
- succinic semialdehyde dehydrogenase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics