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1nof
From Proteopedia
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THE FIRST CRYSTALLOGRAPHIC STRUCTURE OF A XYLANASE FROM GLYCOSYL HYDROLASE FAMILY 5: IMPLICATIONS FOR CATALYSIS
Overview
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.
About this Structure
1NOF is a Single protein structure of sequence from Erwinia chrysanthemi with ACT as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis., Larson SB, Day J, Barba de la Rosa AP, Keen NT, McPherson A, Biochemistry. 2003 Jul 22;42(28):8411-22. PMID:12859186
Page seeded by OCA on Tue Dec 18 16:49:29 2007
