User:Cboursnell/Sandbox/6PGD

From Wikipedia, the free encyclopedia
6PGD
crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for nadp specificity and the enzyme mechanism
Identifiers
Symbol6PGD
PfamPF00393
Pfam clanCL0106
InterProIPR006114
PROSITEPDOC00390
SCOP22pgd / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

6-Phosphogluconate dehydrogenase (EC) (6PGD) is an oxidative carboxylase that catalyses the decarboxylating reduction of 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP. This reaction is a component of the hexose mono-phosphate shunt and pentose phosphate pathways (PPP).[1][2] Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequences are highly conserved.[3] The protein is a homodimer in which the monomers act independently [2]: each contains a large, mainly alpha-helical domain and a smaller beta-alpha-beta domain, containing a mixed parallel and anti-parallel 6-stranded beta sheet.[2] NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket.[2]

This entry represents the C-terminal all-alpha domain of 6-phosphogluconate dehydrogenase. The domain contains two structural repeats of 5 helices each. The NAD-binding domain is described in INTERPRO.


References[edit]

  1. ^ Broedel SE, Wolf RE (July 1990). "Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase". J. Bacteriol. 172 (7): 4023–4031. doi:10.1128/jb.172.7.4023-4031.1990. PMC 213388. PMID 2113917.{{cite journal}}: CS1 maint: date and year (link)
  2. ^ a b c d Adams MJ, Archibald IG, Bugg CE, Carne A, Gover S, Helliwell JR, Pickersgill RW, White SW (1983). "The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution". EMBO J. 2 (6): 1009–1014. doi:10.1002/j.1460-2075.1983.tb01535.x. PMC 555222. PMID 6641716.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ Reizer A, Deutscher J, Saier MH, Reizer J (May 1991). "Analysis of the gluconate (gnt) operon of Bacillus subtilis". Mol. Microbiol. 5 (5): 1081–1089. doi:10.1111/j.1365-2958.1991.tb01880.x. PMID 1659648.{{cite journal}}: CS1 maint: date and year (link) CS1 maint: multiple names: authors list (link)
This article incorporates text from the public domain Pfam and InterPro: IPR006114

Category:Protein domains