1vbr
Crystal structure of complex xylanase 10B from Thermotoga maritima with xylobiose
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OverviewOverview
The crystal structure of xylanase 10B from Thermotoga maritima MSB8, (TmxB), a hyperthermostable xylanase, has been solved in its native form, and in complex with xylobiose or xylotriose at 1.8 A resolution. In order, to gain insight into the substrate subsite and the molecular features for, thermal stability, we compared TmxB with family 10 xylanase structures, from nine microorganisms. As expected, TmxB folds into a, (beta/alpha)8-barrel structure, which is common among the glycoside, hydrolase family 10. The enzyme active site and the environment, surrounding the xylooligosaccharide of TmxB are highly similar to those of, family 10 xylanases. However, only two xylose moieties were found in its, binding pocket from the TmxB-xylotriose complex structure. This finding, suggests that TmxB could be a potential biocatalyst for the large-scale, production of xylobiose. The result of structural analyses also indicated, that TmxB possesses some additional features that account for its, thermostability. In particular, clusters of aromatic residues together, with a lack of exposed hydrophobic residues are characteristic of the TmxB, structure. TmxB has also a significant number of ion pairs on the protein, surface that are not found in other thermophilic family 10 xylanases.
About this StructureAbout this Structure
1VBR is a Single protein structure of sequence from Thermotoga maritima with ACY as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8., Ihsanawati, Kumasaka T, Kaneko T, Morokuma C, Yatsunami R, Sato T, Nakamura S, Tanaka N, Proteins. 2005 Dec 1;61(4):999-1009. PMID:16247799
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