Crystallization and preliminary X-ray crystallographic studies of succinic semialdehyde dehydrogenase from Streptococcus pyogenes

Eun Hyuk Jang, Jong Eun Lim, Young Min Chi, Ki Seog Lee

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2 Citations (Scopus)

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 languageEnglish
Pages (from-to)288-291
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number3
DOIs
Publication statusPublished - 2012 Mar 1

Fingerprint

Succinate-Semialdehyde Dehydrogenase
streptococcus
dehydrogenases
Streptococcus pyogenes
Crystallization
NAD
X-Rays
crystallization
X rays
Crystals
Apoenzymes
crystals
Aminobutyrates
Synchrotrons
x rays
Succinic Acid
gamma-Aminobutyric Acid
Neurotransmitter Agents
neurotransmitters
acids

Keywords

  • GabD
  • NAD
  • Streptococcus pyogenes
  • succinic semialdehyde dehydrogenase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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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 {\AA}, 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 {\AA} for the native crystal and a = 93.3, b = 100.3, c = 105.0 {\AA} 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 {\AA} 3 Da -1 and a solvent content of 48.0{\%}.",
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AU - Jang, Eun Hyuk

AU - Lim, Jong Eun

AU - Chi, Young Min

AU - Lee, Ki Seog

PY - 2012/3/1

Y1 - 2012/3/1

N2 - 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%.

AB - 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%.

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