16 research outputs found
Characterization of different crystal forms of the α-glucosidase MalA from \u3ci\u3eSulfolobus solfataricus\u3c/i\u3e
MalA is an _-glucosidase from the hyperthermophilic archaeon Sulfolobus
solfataricus. It belongs to glycoside hydrolase family 31, which includes several
medically interesting α-glucosidases. MalA and its selenomethionine derivative
have been overproduced in Escherichia coli and crystallized in four different
crystal forms. Microseeding was essential for the formation of good-quality
crystals of forms 2 and 4. For three of the crystal forms (2, 3 and 4) full data sets
could be collected. The most suitable crystals for structure determination are the
monoclinic form 4 crystals, belonging to space group P21, from which data sets
extending to 2.5 Å resolution have been collected. Self-rotation functions
calculated for this form and for the orthorhombic (P212121) form 2 indicate the
presence of six molecules in the asymmetric unit related by 32 symmetry
Characterization of different crystal forms of the α-glucosidase MalA from \u3ci\u3eSulfolobus solfataricus\u3c/i\u3e
MalA is an _-glucosidase from the hyperthermophilic archaeon Sulfolobus
solfataricus. It belongs to glycoside hydrolase family 31, which includes several
medically interesting α-glucosidases. MalA and its selenomethionine derivative
have been overproduced in Escherichia coli and crystallized in four different
crystal forms. Microseeding was essential for the formation of good-quality
crystals of forms 2 and 4. For three of the crystal forms (2, 3 and 4) full data sets
could be collected. The most suitable crystals for structure determination are the
monoclinic form 4 crystals, belonging to space group P21, from which data sets
extending to 2.5 Å resolution have been collected. Self-rotation functions
calculated for this form and for the orthorhombic (P212121) form 2 indicate the
presence of six molecules in the asymmetric unit related by 32 symmetry
Origin and evolution of transporter substrate specificity within the NPF family
Despite vast diversity in metabolites and the matching substrate specificity of their transporters, little is known about how evolution of transporter substrate specificities is linked to emergence of substrates via evolution of biosynthetic pathways. Transporter specificity towards the recently evolved glucosinolates characteristic of Brassicales is shown to evolve prior to emergence of glucosinolate biosynthesis. Furthermore, we show that glucosinolate transporters belonging to the ubiquitous NRT1/PTR FAMILY (NPF) likely evolved from transporters of the ancestral cyanogenic glucosides found across more than 2500 species outside of the Brassicales. Biochemical characterization of orthologs along the phylogenetic lineage from cassava to A. thaliana, suggests that alterations in the electrogenicity of the transporters accompanied changes in substrate specificity. Linking the evolutionary path of transporter substrate specificities to that of the biosynthetic pathways, exemplify how transporter substrate specificities originate and evolve as new biosynthesis pathways emerge
An Optimized Screen Reduces the Number of GA Transporters and Provides Insights Into Nitrate Transporter 1/Peptide Transporter Family Substrate Determinants
A structural model for the N-terminal N1 module of <em>E. coli</em> glycogen branching enzyme
Crystallization and preliminary X-ray analysis of <em>Alicyclobacillus acidocaldarius</em> endoglucanase CelA
Characterization of different crystal forms of the a-glucosidase MalA from <em>Sulfolobus solfataricus</em>
Characterization of different crystal forms of the α-glucosidase MalA from Sulfolobus solfataricus
Crystallization of the α-glucosidase MalA from S. solfataricus belonging to glycoside hydrolase family 31