1vbu
From Proteopedia
(New page: 200px<br /><applet load="1vbu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vbu, resolution 1.80Å" /> '''Crystal structure of...) |
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| - | [[Image:1vbu.gif|left|200px]]<br /><applet load="1vbu" size=" | + | [[Image:1vbu.gif|left|200px]]<br /><applet load="1vbu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vbu, resolution 1.80Å" /> | caption="1vbu, resolution 1.80Å" /> | ||
'''Crystal structure of native xylanase 10B from Thermotoga maritima'''<br /> | '''Crystal structure of native xylanase 10B from Thermotoga maritima'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of xylanase 10B from Thermotoga maritima MSB8 | + | 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== | ==About this Structure== | ||
| - | 1VBU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4, ACY and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Full crystallographic information is available from [http:// | + | 1VBU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ACY:'>ACY</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VBU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylanase 10b]] | [[Category: xylanase 10b]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:39 2008'' |
Revision as of 13:33, 21 February 2008
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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 with , and as ligands. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 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 Thu Feb 21 15:33:39 2008
Categories: Endo-1,4-beta-xylanase | Single protein | Thermotoga maritima | Ihsanawati | Kaneko, T. | Kumasaka, T. | Nakamura, S. | Tanaka, N. | ACY | GOL | SO4 | Xylanase 10b
