PDBsum entry: 1r7a

Transferase

PDB id: 1r7a

Contents

Protein chains

504 a.a. *

Ligands

TRS ×2

Waters ×1421

* Residue conservation analysis

PDB id:

1r7a

Name:

Transferase

Title:

Sucrose phosphorylase from bifidobacterium adolescentis

Structure:

Sucrose phosphorylase. Chain: a, b. Engineered: yes

Source:

Bifidobacterium adolescentis. Organism_taxid: 1680. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.77Å R-factor: 0.164 R-free: 0.195

Authors:

D.Sprogoe,L.A.M.Van Den Broek,O.Mirza,J.S.Kastrup, A.G.J.Voragen,M.Gajhede,L.K.Skov

Key ref:

D.Sprogøe et al. (2004). Crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis. Biochemistry, 43, 1156-1162. PubMed id: 14756551 DOI: 10.1021/bi0356395

Date:

21-Oct-03 Release date: 10-Feb-04

Protein chains

Q84HQ2  (Q84HQ2_BIFAD) -  Sucrose phosphorylase

Seq: 504 a.a.

Struc: 504 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.4.1.7 - Sucrose phosphorylase.
• Reaction: Sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: carbohydrate metabolic process (2 terms)
• Biochemical function: catalytic activity (5 terms)

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.