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3JZ4

Crystal structure of E. coli NADP dependent enzyme

Summary for 3JZ4
Entry DOI10.2210/pdb3jz4/pdb
DescriptorSuccinate-semialdehyde dehydrogenase [NADP+], NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
Functional Keywordstetramer, nadp binding, nadp, oxidoreductase
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight209684.50
Authors
Langendorf, C.G.,Key, T.L.G.,Fenalti, G.,Kan, W.T.,Buckle, A.M.,Caradoc-Davies, T.,Tuck, K.L.,Law, R.H.P.,Whisstock, J.C. (deposition date: 2009-09-22, release date: 2010-03-16, Last modification date: 2024-02-21)
Primary citationLangendorf, C.G.,Key, T.L.,Fenalti, G.,Kan, W.T.,Buckle, A.M.,Caradoc-Davies, T.,Tuck, K.L.,Law, R.H.,Whisstock, J.C.
The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions.
Plos One, 5:e9280-e9280, 2010
Cited by
PubMed Abstract: In mammals succinic semialdehyde dehydrogenase (SSADH) plays an essential role in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) to succinic acid (SA). Deficiency of SSADH in humans results in elevated levels of GABA and gamma-Hydroxybutyric acid (GHB), which leads to psychomotor retardation, muscular hypotonia, non-progressive ataxia and seizures. In Escherichia coli, two genetically distinct forms of SSADHs had been described that are essential for preventing accumulation of toxic levels of succinic semialdehyde (SSA) in cells.
PubMed: 20174634
DOI: 10.1371/journal.pone.0009280
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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