| http://purl.uniprot.org/citations/15292273 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15292273 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15292273 | http://www.w3.org/2000/01/rdf-schema#comment | "As the first known structures of a glycoside hydrolase family 54 (GH54) enzyme, we determined the crystal structures of free and arabinose-complex forms of Aspergillus kawachii IFO4308 alpha-l-arabinofuranosidase (AkAbfB). AkAbfB comprises two domains: a catalytic domain and an arabinose-binding domain (ABD). The catalytic domain has a beta-sandwich fold similar to those of clan-B glycoside hydrolases. ABD has a beta-trefoil fold similar to that of carbohydrate-binding module (CBM) family 13. However, ABD shows a number of characteristics distinctive from those of CBM family 13, suggesting that it could be classified into a new CBM family. In the arabinose-complex structure, one of three arabinofuranose molecules is bound to the catalytic domain through many interactions. Interestingly, a disulfide bond formed between two adjacent cysteine residues recognized the arabinofuranose molecule in the active site. From the location of this arabinofuranose and the results of a mutational study, the nucleophile and acid/base residues were determined to be Glu(221) and Asp(297), respectively. The other two arabinofuranose molecules are bound to ABD. The O-1 atoms of the two arabinofuranose molecules bound at ABD are both pointed toward the solvent, indicating that these sites can both accommodate an arabinofuranose side-chain moiety linked to decorated arabinoxylans."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m405390200"xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m405390200"xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Fushinobu S."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Fushinobu S."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Koseki T."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Koseki T."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Shoun H."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Shoun H."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Wakagi T."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Wakagi T."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Matsuzawa H."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Matsuzawa H."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Miyanaga A."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/author | "Miyanaga A."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/pages | "44907-44914"xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/pages | "44907-44914"xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/title | "Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose."xsd:string |
| http://purl.uniprot.org/citations/15292273 | http://purl.uniprot.org/core/title | "Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose."xsd:string |