title: Crystallization and preliminary X-ray crystallographic studies of succinic semialdehyde dehydrogenase from Streptococcus pyogenes.
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(1)2(1)2(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%.
authors.affiliation: Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-713, Republic of Korea.
authors.forename: Eun Hyuk
authors.initials: EH
authors.lastname: Jang
authors.forename: Jong Eun
authors.initials: JE
authors.lastname: Lim
authors.forename: Young Min
authors.initials: YM
authors.lastname: Chi
authors.forename: Ki Seog
authors.initials: KS
authors.lastname: Lee
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D013297:Streptococcus pyogenes / Q000201:enzymology*; D050644:Succinate-Semialdehyde Dehydrogenase / Q000737:chemistry*
chemical_list: D050644:Succinate-Semialdehyde Dehydrogenase