The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan.
FEBS Lett
; 579(20): 4324-8, 2005 Aug 15.
Article
em En
| MEDLINE
| ID: mdl-16061225
ABSTRACT
Here, we present the crystal structure of the family 31 carbohydrate-binding module (CBM) of beta-1,3-xylanase from Alcaligenes sp. strain XY-234 (AlcCBM31) determined at a resolution of 1.25A. The AlcCBM31 shows affinity with only beta-1,3-xylan. The AlcCBM31 molecule makes a beta-sandwich structure composed of eight beta-strands with a typical immunoglobulin fold and contains two intra-molecular disulfide bonds. The folding topology of AlcCBM31 differs from that of the large majority of other CBMs, in which eight beta-strands comprise a beta-sandwich structure with a typical jelly-roll fold. AlcCBM31 shows structural similarity with CBM structures of family 34 and family 9, which also adopt structures based on immunoglobulin folds.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Xilanos
/
Xilano Endo-1,3-beta-Xilosidase
/
Alcaligenes
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article