1nof: Difference between revisions
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THE FIRST CRYSTALLOGRAPHIC STRUCTURE OF A XYLANASE FROM GLYCOSYL HYDROLASE FAMILY 5: IMPLICATIONS FOR CATALYSIS
OverviewOverview
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, ... [(full description)]
About this StructureAbout 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]. Structure known Active Sites: ACI and NUC. Full crystallographic information is available from [OCA].
ReferenceReference
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
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