spacer
spacer

PDBsum entry 3jz4

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3jz4
Jmol
Contents
Protein chains
481 a.a. *
Ligands
NAP ×4
Waters ×331
* Residue conservation analysis
PDB id:
3jz4
Name: Oxidoreductase
Title: Crystal structure of e. Coli NADP dependent enzyme
Structure: Succinate-semialdehyde dehydrogenase [nadp+]. Chain: a, b, c, d. Synonym: ssdh, NADP dependent enzyme. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Strain: mc1061. Gene: b2661, gabd, jw2636, na. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.30Å     R-factor:   0.170     R-free:   0.213
Authors: C.G.Langendorf,T.L.G.Key,G.Fenalti,W.T.Kan,A.M.Buckle,T.Cara Davies,K.L.Tuck,R.H.P.Law,J.C.Whisstock
Key ref: C.G.Langendorf et al. (2010). The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions. PLoS One, 5, e9280. PubMed id: 20174634
Date:
22-Sep-09     Release date:   16-Mar-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P25526  (GABD_ECOLI) -  Succinate-semialdehyde dehydrogenase [NADP(+)] GabD
Seq:
Struc:
482 a.a.
481 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.2.1.79  - Succinate-semialdehyde dehydrogenase (NADP(+)).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Succinate semialdehyde + NADP+ + H2O = succinate + NADPH
Succinate semialdehyde
+
NADP(+)
Bound ligand (Het Group name = NAP)
corresponds exactly
+ H(2)O
= succinate
+ NADPH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     metabolic process   4 terms 
  Biochemical function     oxidoreductase activity     4 terms  

 

 
    reference    
 
 
PLoS One 5:e9280 (2010)
PubMed id: 20174634  
 
 
The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions.
C.G.Langendorf, T.L.Key, G.Fenalti, W.T.Kan, A.M.Buckle, T.Caradoc-Davies, K.L.Tuck, R.H.Law, J.C.Whisstock.
 
  ABSTRACT  
 
BACKGROUND: 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. METHODOLOGY/PRINCIPAL FINDINGS: Here we structurally characterise SSADH encoded by the E coli gabD gene by X-ray crystallographic studies and compare these data with the structure of human SSADH. In the E. coli SSADH structure, electron density for the complete NADP+ cofactor in the binding sites is clearly evident; these data in particular revealing how the nicotinamide ring of the cofactor is positioned in each active site. CONCLUSIONS/SIGNIFICANCE: Our structural data suggest that a deletion of three amino acids in E. coli SSADH permits this enzyme to use NADP+, whereas in contrast the human enzyme utilises NAD+. Furthermore, the structure of E. coli SSADH gives additional insight into human mutations that result in disease.