Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2D44

Crystal structure of arabinofuranosidase complexed with arabinofuranosyl-alpha-1,2-xylobiose

Summary for 2D44
Entry DOI10.2210/pdb2d44/pdb
Related1WD3 1WD4 2D43
Descriptoralpha-L-arabinofuranosidase B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-arabinofuranose-(1-2)-alpha-D-xylopyranose-(1-4)-alpha-D-xylopyranose, ... (4 entities in total)
Functional Keywordsarabinofuranosyl-alpha-1, 2-xylobiose complex, hydrolase, structural genomics
Biological sourceAspergillus kawachii
Total number of polymer chains1
Total formula weight52078.63
Authors
Miyanaga, A.,Koseki, T.,Miwa, Y.,Matsuzawa, H.,Wakagi, T.,Shoun, H.,Fushinobu, S. (deposition date: 2005-10-07, release date: 2006-09-19, Last modification date: 2021-11-10)
Primary citationMiyanaga, A.,Koseki, T.,Miwa, Y.,Mese, Y.,Nakamura, S.,Kuno, A.,Hirabayashi, J.,Matsuzawa, H.,Wakagi, T.,Shoun, H.,Fushinobu, S.
The family 42 carbohydrate-binding module of family 54 alpha-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose
Biochem.J., 399:503-511, 2006
Cited by
PubMed Abstract: Alpha-L-arabinofuranosidase catalyses the hydrolysis of the alpha-1,2-, alpha-1,3-, and alpha-1,5-L-arabinofuranosidic bonds in L-arabinose-containing hemicelluloses such as arabinoxylan. AkAbf54 (the glycoside hydrolase family 54 alpha-L-arabinofuranosidase from Aspergillus kawachii) consists of two domains, a catalytic and an arabinose-binding domain. The latter has been named AkCBM42 [family 42 CBM (carbohydrate-binding module) of AkAbf54] because homologous domains are classified into CBM family 42. In the complex between AkAbf54 and arabinofuranosyl-alpha-1,2-xylobiose, the arabinose moiety occupies the binding pocket of AkCBM42, whereas the xylobiose moiety is exposed to the solvent. AkCBM42 was found to facilitate the hydrolysis of insoluble arabinoxylan, because mutants at the arabinose binding site exhibited markedly decreased activity. The results of binding assays and affinity gel electrophoresis showed that AkCBM42 interacts with arabinose-substituted, but not with unsubstituted, hemicelluloses. Isothermal titration calorimetry and frontal affinity chromatography analyses showed that the association constant of AkCBM42 with the arabinose moiety is approximately 10(3) M(-1). These results indicate that AkCBM42 binds the non-reducing-end arabinofuranosidic moiety of hemicellulose. To our knowledge, this is the first example of a CBM that can specifically recognize the side-chain monosaccharides of branched hemicelluloses.
PubMed: 16846393
DOI: 10.1042/BJ20060567
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon