Trimeric Crystal Structure of the Glycoside Hydrolase Family 42 β-Galactosidase from Thermus thermophilus A4 and the Structure of its Complex with Galactose

Hidaka, Masafumi; Fushinobu, Shinya; Ohtsu, Naomi; Motoshima, Hidemasa; Matsuzawa, Hiroshi; Shoun, Hirofumi; Wakagi, Takayoshi

doi:10.1016/s0022-2836(02)00746-5

Cited by 107 publications

(124 citation statements)

References 52 publications

Supporting

Mentioning

114

Contrasting

Unclassified

Order By: Relevance

“…Each monomer of A4 ␤-Gal has an active site located inside a large central tunnel formed by the interface of the trimer (28). The active site of human ␤-Gal is easily accessible from the bulk solvent, in contrast to the active sites of A4 ␤-Gal, C221 ␤-Gal, and EC ␤-Gal, which are segregated from the bulk solvent.…”

Section: Resultsmentioning

confidence: 99%

Crystal Structure of Human β-Galactosidase

Ohto¹,

Usui²,

Ochi

et al. 2012

Journal of Biological Chemistry

102

View full text Add to dashboard Cite

Background: Deficiencies in ␤-D-galactosidase cause lysosomal storage diseases. Results: This is the first report to describe the crystal structure of human ␤-Gal. Human ␤-Gal is composed of a TIM barrel domain and two ␤-domains. Conclusion: The mutations were classified as mutations directly affecting the ligand recognition, mutations inside the protein core, or mutations located in the protein surface. Significance: Structural insights into lysosomal storage diseases mutations can be demonstrated.

show abstract

Section: Resultsmentioning

confidence: 99%

Crystal Structure of Human β-Galactosidase

Ohto¹,

Usui²,

Ochi

et al. 2012

Journal of Biological Chemistry

102

View full text Add to dashboard Cite

show abstract

“…Another interesting overlap was observed between Arg-32 of GLNBP (anion binding) and Arg-32 in A4-␤-galactosidase, both being located at the same position in the barrel (␤2 strand). Arg-32 in A4-␤-galactosidase is a highly conserved residue and is considered to control the pK a of the nucleophile residue (62,63).…”

Section: Discussionmentioning

confidence: 99%

The Crystal Structure of Galacto-N-biose/Lacto-N-biose I Phosphorylase

Hidaka

Nishimoto

Kitaoka

et al. 2009

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

. GLNBP homologues are often found in human pathogenic and commensal bacteria, and their substrate specificities potentially define the nutritional acquisition ability of these microbes in their habitat. We report the crystal structures of GLNBP in five different ligand-binding forms. This is the first three-dimensional structure of glycoside hydrolase (GH) family 112. The GlcNAc-and GalNAc-bound forms provide structural insights into distinct substrate preferences of GLNBP and its homologues from pathogens. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a thermophilic ␤-galactosidase, strongly supporting the current classification of GLNBP homologues as one of the GH families. Anion binding induces a large conformational change by rotating a half-unit of the barrel. This is an unusual example of molecular adaptation of a TIM barrel scaffold to substrates.

show abstract

“…13) GH A is the largest clan formed by 17 GH families, all of which are retaining enzymes. The closest structural neighbor of the catalytic domain of A4 β Gal is, however, not a clan GH A enzyme, 7) but the GH14 inverting β amylase from Bacillus cereus 14) (Fig. 2).…”

Section: Gh42: a Possible Link Between Retaining And Invert-mentioning

confidence: 99%

“…6) Our group has been trying to solve crystal structures of useful enzymes for use in bioindustry. Two of these were the first crystal structures within the GH42 and GH57 families, 7,8) and we then began to focus on CAZy enzymes belonging to structurally unknown families. We have since solved two more GH families, and provided the first crystal structures within GH54 and GH94.…”

mentioning

confidence: 99%

New Structural Insights on Carbohydrate-active Enzymes

Fushinobu¹,

Hidaka²,

Miyanaga³

et al. 2007

J. Appl. Glycosci.

Self Cite

View full text Add to dashboard Cite

Polysaccharides show a huge degree of diversity owing to their variety of sugar components (aldoses, ketoses and their stereoisomers), the variety of glycosidic bonds (e.g., α 1,4 , α 1,6 , β 1,4 , β 1,3 , etc.), different degrees of polymerization, and different degrees of branching. Therefore, they can be involved in many types of biological function with distinct physicochemical characteristics. It is especially intriguing that α and β glucans, such as amylose (starch) and cellulose, are built from the same glucose units, differing only in the anomeric configurations of glycosidic bonds. Enzymes that hydrolyze these glucans, amylases and cellulases, are the two largest groups of glycoside hydrolases, and have been studied for a long time. A framework to discuss a whole variety of glycoside hydrolases with their three dimensional structural aspects has been established within the last 15 years. In the late 1980s, Henrissat et al. began classification of the amino acid sequences of enzymes, focusing on cellulases and hemicellulases. 1) At the earliest stage of their classification, the α amylase family was treated as belonging to a separate system.2) In 1991, the naming system of the families changed from alphabetical to numerical, and the system expanded to 35 "glycosyl hydrolase" families, incorporating three well known amylase families, GH13 (retaining α amylase family), GH14 (inverting β amylase family), and GH15 (inverting glucoamylase family), as well as many other enzymes.3) All enzymes cleaving, modifying, and creating glycosidic bonds, and modules binding to carbohydrates have been incorporated into the CAZy database (http: www.cazy.org CAZY ). Glycoside hydrolase (GH) families now include enzymes that hydrolyze the glycosidic bonds between two or more carbohydrates or between a carbohydrate and a non carbohydrate moiety. At present, there are 101 families in the GH class ( Fig. 1; note, five have been deleted or reassigned to other classes), and it will continue to grow.The first 3 D structure of a glycoside hydrolase to be determined was that of hen egg white lysozyme (classified into GH22) in the mid 1960s.4) Even in the early 1990s, however, only a limited number of GH enzyme structures were available. Henrissat and colleagues took amino acid sequence information as the primary basis for classification, but they also used hydrophobic cluster analysis from the earliest stage, trying to incorporate as much 3 D structure based information as possible.5) The significant advances in structural studies of GH enzymes over the last decade have indicated that these enzymes show a vast array of tertiary scaffolds, described as "a marketplace of different structures". 6)Our group has been trying to solve crystal structures of useful enzymes for use in bioindustry. Two of these were the first crystal structures within the GH42 and GH57 families, 7,8) and we then began to focus on CAZy enzymes belonging to structurally unknown families. We have since solved two more GH families, and provided the first crystal s...

show abstract

Trimeric Crystal Structure of the Glycoside Hydrolase Family 42 β-Galactosidase from Thermus thermophilus A4 and the Structure of its Complex with Galactose

Cited by 107 publications

References 52 publications

Crystal Structure of Human β-Galactosidase

Crystal Structure of Human β-Galactosidase

The Crystal Structure of Galacto-N-biose/Lacto-N-biose I Phosphorylase

New Structural Insights on Carbohydrate-active Enzymes

Contact Info

Product

Resources

About