1NOF

THE FIRST CRYSTALLOGRAPHIC STRUCTURE OF A XYLANASE FROM GLYCOSYL HYDROLASE FAMILY 5: IMPLICATIONS FOR CATALYSIS

Summary for 1NOF

• Entry DOI: 10.2210/pdb1nof/pdb
• Descriptor: xylanase, ACETATE ION (3 entities in total)
• Functional Keywords: xylanase, glycohydrolase family 5, carbohydrate-binding module, catalytic domain, hydrolase
• Biological source: Erwinia chrysanthemi
• Total number of polymer chains: 1
• Total formula weight: 42131.06

Authors

Larson, S.B.,Day, J.,McPherson, A.,Barba De La Rosa, A.P.,Keen, N.T. (deposition date: 2003-01-16, release date: 2003-09-16, Last modification date: 2024-02-14)

Primary citation

Larson, S.B.,Day, J.,Barba de la Rosa, A.P.,Keen, N.T.,McPherson, A.
First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis.
Biochemistry, 42:8411-8422, 2003

PubMed Abstract: The room-temperature structure of xylanase (EC 3.2.1.8) from the bacterial plant pathogen Erwinia chrysanthemi expressed in Escherichia coli, a 45 kDa, 413-amino acid protein belonging to glycoside hydrolase family 5, has been determined by multiple isomorphous replacement and refined to a resolution of 1.42 A. This represents the first structure of a xylanase not belonging to either glycoside hydrolase family 10 or family 11. The enzyme is composed of two domains similar to most family 10 xylanases and the alpha-amylases. The catalytic domain (residues 46-315) has a (beta/alpha)(8)-barrel motif with a binding cleft along the C-terminal side of the beta-barrel. The catalytic residues, Glu165 and Glu253, determined by correspondence to other family 5 and family 10 glycoside hydrolases, lie inside this cleft on the C-terminal ends of beta-strands 4 and 7, respectively, with an O(epsilon)2...O(epsilon)1 distance of 4.22 A. The smaller domain (residues 31-43 and 323-413) has a beta(9)-barrel motif with five of the strands interfacing with alpha-helices 7 and 8 of the catalytic domain. The first 13 N-terminal residues form one beta-strand of this domain. Residues 44, 45, and 316-322 form the linkers between this domain and the catalytic domain.

PubMed: 12859186
DOI: 10.1021/bi034144c

Experimental method

X-RAY DIFFRACTION (1.42 Å)