1vbu

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[[Image:1vbu.gif|left|200px]]<br /><applet load="1vbu" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vbu.gif|left|200px]]
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caption="1vbu, resolution 1.80&Aring;" />
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'''Crystal structure of native xylanase 10B from Thermotoga maritima'''<br />
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{{Structure
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|PDB= 1vbu |SIZE=350|CAPTION= <scene name='initialview01'>1vbu</scene>, resolution 1.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Crystal structure of native xylanase 10B from Thermotoga maritima'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1VBU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VBU OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16247799 16247799]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16247799 16247799]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: xylanase 10b]]
[[Category: xylanase 10b]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:43:31 2008''

Revision as of 12:43, 20 March 2008


PDB ID 1vbu

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands: , and
Activity: Endo-1,4-beta-xylanase, with EC number 3.2.1.8
Coordinates: save as pdb, mmCIF, xml



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

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