 |
|
|
 |
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
504 a.a.
 Sucrose |
+ |
 phosphate |
= |
 D-fructose |
+ |
 alpha-D-glucose 1-phosphate |
|---|
Key reference
DOI no: 10.1021/bi0356395 Biochemistry 43:1156-1162 (2004) PubMed id: 14756551
Crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis. D.Sprogøe, L.A.van den Broek, O.Mirza, J.S.Kastrup, A.G.Voragen, M.Gajhede, L.K.Skov. ABSTRACT
Around 80 enzymes are implicated in the generic starch and sucrose pathways. One of these enzymes is sucrose phosphorylase, which reversibly catalyzes the conversion of sucrose and orthophosphate to d-Fructose and alpha-d-glucose 1-phosphate. Here, we present the crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis (BiSP) refined at 1.77 A resolution. It represents the first 3D structure of a sucrose phosphorylase and is the first structure of a phosphate-dependent enzyme from the glycoside hydrolase family 13. The structure of BiSP is composed of the four domains A, B, B', and C. Domain A comprises the (beta/alpha)(8)-barrel common to family 13. The catalytic active-site residues (Asp192 and Glu232) are located at the tips of beta-sheets 4 and 5 in the (beta/alpha)(8)-barrel, as required for family 13 members. The topology of the B' domain disfavors oligosaccharide binding and reduces the size of the substrate access channel compared to other family 13 members, underlining the role of this domain in modulating the function of these enzymes. It is remarkable that the fold of the C domain is not observed in any other known hydrolases of family 13. BiSP was found as a homodimer in the crystal, and a dimer contact surface area of 960 A(2) per monomer was calculated. The majority of the interactions are confined to the two B domains, but interactions between the loop 8 regions of the two barrels are also observed. This results in a large cavity in the dimer, including the entrance to the two active sites.
Literature references that cite this PDB file's key reference
PubMed id Reference
18040988 L.A.van den Broek, S.W.Hinz, G.Beldman, J.P.Vincken, and A.G.Voragen (2008).
Bifidobacterium carbohydrases-their role in breakdown and synthesis of (potential) prebiotics.Mol Nutr Food Res, 52, 146-163.
16523284 B.Kullin, V.R.Abratt, and S.J.Reid (2006).
A functional analysis of the Bifidobacterium longum cscA and scrP genes in sucrose utilization.Appl Microbiol Biotechnol, 72, 975-981.
16990265 O.Mirza, L.K.Skov, D.Sprogøe, L.A.van den Broek, G.Beldman, J.S.Kastrup, and M.Gajhede (2006).
Structural rearrangements of sucrose phosphorylase from Bifidobacterium adolescentis during sucrose conversion.J Biol Chem, 281, 35576-35584.
PDB codes: 2gdu 2gdv
15660210 S.J.Reid, and V.R.Abratt (2005).
Sucrose utilisation in bacteria: genetic organisation and regulation.Appl Microbiol Biotechnol, 67, 312-321.
15375133 C.I.Caescu, O.Vidal, F.Krzewinski, V.Artenie, and S.Bouquelet (2004).
Bifidobacterium longum requires a fructokinase (Frk; ATP:D-fructose 6-phosphotransferase, EC 2.7.1.4) for fructose catabolism.J Bacteriol, 186, 6515-6525. The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.
