1QLD

Solution structure of type X CBM

Summary for 1QLD

• Entry DOI: 10.2210/pdb1qld/pdb
• Related: 1CLX 1CT7 1XYS
• Descriptor: XYLANASE (1 entity in total)
• Functional Keywords: xylanase, beta strands, anti parallel beta sheets, xylan degradation, hydrolase, glycosidase
• Biological source: PSEUDOMONAS FLUORESCENS
• Total number of polymer chains: 1
• Total formula weight: 5400.01

Authors

Raghothama, S.,Simpson, P.J.,Gilbert, H.J.,Williamson, M.P. (deposition date: 1999-08-26, release date: 2000-02-06, Last modification date: 2024-10-16)

Primary citation

Raghothama, S.,Simpson, P.J.,Szabo, L.,Nagy, T.,Gilbert, H.J.,Williamson, M.P.
Solution Structure of Cbm10 Cellulose Binding Module from Pseudomonas Xylanase A
Biochemistry, 39:978-, 2000

PubMed Abstract: Plant cell wall hydrolases generally have a modular structure consisting of a catalytic domain linked to one or more noncatalytic carbohydrate-binding modules (CBMs), whose common function is to attach the enzyme to the polymeric substrate. Xylanase A from Pseudomonas fluorescens subsp. cellulosa (Pf Xyn10A) consists of a family 10 catalytic domain, an N-terminal family IIa cellulose-binding module, and an internal family 10 cellulose-binding module. The structure of the 45-residue family 10 CBM has been determined in solution using NMR. It consists of two antiparallel beta-sheets, one with two strands and one with three, with a short alpha-helix across one face of the three-stranded sheet. There is a high density of aromatic residues on one side of the protein, including three aromatic residues (Tyr8, Trp22, and Trp24), which are exposed and form a flat surface on one face, in a classical polysaccharide-binding arrangement. The fold is closely similar to that of the oligonucleotide/oligosaccharide-binding (OB) fold, but appears to have arisen by convergent evolution, because there is no sequence similarity, and the presumed binding sites are on different faces.

PubMed: 10653641
DOI: 10.1021/BI992163+

Experimental method

SOLUTION NMR