6PWQ

Crystal structure of Levansucrase from Bacillus subtilis mutant S164A at 2.6 A

Summary for 6PWQ

• Entry DOI: 10.2210/pdb6pwq/pdb
• Descriptor: Glycoside hydrolase family 68 protein, CALCIUM ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: levansucrase, transferase, glycoside hydrolase, levan, fructose polymers
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 107744.03

Authors

Diaz-Vilchis, A.,Rodriguez-Alegria, M.E.,Ortiz-Soto, M.E.,Rudino-Pinera, E.,Lopez-Munguia, A. (deposition date: 2019-07-23, release date: 2020-07-22, Last modification date: 2023-10-11)

Primary citation

Ortiz-Soto, M.E.,Porras-Dominguez, J.R.,Rodriguez-Alegria, M.E.,Morales-Moreno, L.A.,Diaz-Vilchis, A.,Rudino-Pinera, E.,Beltran-Hernandez, N.E.,Rivera, H.M.,Seibel, J.,Lopez Munguia, A.
Implications of the mutation S164A on Bacillus subtilis levansucrase product specificity and insights into protein interactions acting upon levan synthesis.
Int.J.Biol.Macromol., 161:898-908, 2020

PubMed Abstract: Mutation S164A largely affects the transfructosylation properties of Bacillus subtilis levansucrase (SacB). The variant uses acceptors such as glucose and short levans with an average molecular weight of 7.6 kDa more efficiently than SacB, leading to the enhanced synthesis of medium and high molecular weight polymer and a blasto-oligosaccharide series with a polymerization degree of 2-10. A 3-fold increase in blasto-oligosaccharides yield is provoked by the modified interplay between the variant and glucose. Despite its modified product specificity, protein-carbohydrate and protein-protein interactions are still a major factor affecting size and distribution of levan molecular weight. This study highlights the importance of critical factors such as protein concentration in the analysis of wild-type and mutagenized levansucrases. Docking experiments with the crystal structures of SacB and variant S164A - the latter obtained at a 2.6 Å resolution - identified unreported potential binding subsites for fructosyl moieties on the surface of both enzymes.

PubMed: 32553967
DOI: 10.1016/j.ijbiomac.2020.06.114

Experimental method

X-RAY DIFFRACTION (2.6 Å)