1ZJB

Crystal structure of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45 (monoclinic form)

Summary for 1ZJB

• Entry DOI: 10.2210/pdb1zjb/pdb
• Related: 1M53 1ZJA
• Descriptor: Trehalulose synthase, CALCIUM ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: trehalulose synthase, sucrose isomerase, alpha-amylase family, (beta/alpha)8 barrel, isomerase
• Biological source: Pseudomonas mesoacidophila
• Total number of polymer chains: 2
• Total formula weight: 128202.14

Authors

Ravaud, S.,Robert, X.,Haser, R.,Aghajari, N. (deposition date: 2005-04-28, release date: 2006-10-17, Last modification date: 2023-08-23)

Primary citation

Ravaud, S.,Watzlawick, H.,Haser, R.,Mattes, R.,Aghajari, N.
Expression, purification, crystallization and preliminary X-ray crystallographic studies of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45.
Acta Crystallogr.,Sect.F, 61:100-103, 2005

PubMed Abstract: The trehalulose synthase (MutB) from Pseudomonas mesoacidophila MX-45, belonging to glycoside hydrolase family 13, catalyses the isomerization of sucrose to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as main products and glucose and fructose in residual amounts from the hydrolytic reaction. To date, a three-dimensional structure of a sucrose isomerase that produces mainly trehalulose, as is the case for MutB, has been lacking. Crystallographic studies of this 64 kDa enzyme have therefore been initiated in order to contribute to the understanding of the molecular basis of sucrose decomposition, isomerization and of the selectivity of this enzyme that leads to the formation of different products. The MutB protein has been overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method. Two different crystal forms have been obtained: one diffracts X-rays to 1.6 A resolution using synchrotron radiation and belongs to space group P1, with unit-cell parameters a = 63.8, b = 72.0, c = 82.2 A, alpha = 67.5, beta = 73.1, gamma = 70.8 degrees, while the other form diffracts to 1.8 A resolution using synchrotron radiation and belongs to space group P2(1), with unit-cell parameters a = 63.7, b = 85.9, c = 119.7 A, beta = 97.7 degrees. A molecular-replacement solution has been found using the structure of the isomaltulose synthase (PalI) from Klebsiella sp. LX3 as a search model.

PubMed: 16508103
DOI: 10.1107/S1744309104030623

Experimental method

X-RAY DIFFRACTION (1.8 Å)