1vbu
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1vbu.gif|left|200px]] | [[Image:1vbu.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1vbu", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1vbu| PDB=1vbu | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''Crystal structure of native xylanase 10B from Thermotoga maritima''' | '''Crystal structure of native xylanase 10B from Thermotoga maritima''' | ||
Line 31: | Line 28: | ||
[[Category: Nakamura, S.]] | [[Category: Nakamura, S.]] | ||
[[Category: Tanaka, N.]] | [[Category: Tanaka, N.]] | ||
- | [[Category: | + | [[Category: Xylanase 10b]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:20:51 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 09:20, 3 May 2008
Crystal structure of native xylanase 10B from Thermotoga maritima
Overview
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 Structure
1VBU is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 12:20:51 2008