3JZ4
Crystal structure of E. coli NADP dependent enzyme
Summary for 3JZ4
Entry DOI | 10.2210/pdb3jz4/pdb |
Descriptor | Succinate-semialdehyde dehydrogenase [NADP+], NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
Functional Keywords | tetramer, nadp binding, nadp, oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 4 |
Total formula weight | 209684.50 |
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 citation | Langendorf, 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: 20174634DOI: 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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