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| [[Image:2bs9.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2bs9| PDB=2bs9 | SCENE= }} | | {{STRUCTURE_2bs9| PDB=2bs9 | SCENE= }} |
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| '''NATIVE CRYSTAL STRUCTURE OF A GH39 BETA-XYLOSIDASE XYNB1 FROM GEOBACILLUS STEAROTHERMOPHILUS'''
| | ===NATIVE CRYSTAL STRUCTURE OF A GH39 BETA-XYLOSIDASE XYNB1 FROM GEOBACILLUS STEAROTHERMOPHILUS=== |
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| ==Overview==
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| Beta-D-Xylosidases are glycoside hydrolases that catalyse the release of xylose units from short xylooligosaccharides and are engaged in the final breakdown of plant cell-wall hemicelluloses. beta-D-Xylosidases are found in glycoside hydrolase families 3, 39, 43, 52 and 54. The first crystal structure of a GH39 beta-xylosidase revealed a multi-domain organization with the catalytic domain having the canonical (beta/alpha)8 barrel fold. Here, we report the crystal structure of the GH39 Geobacillus stearothermophilus beta-D-xylosidase, inactivated by a point mutation of the general acid-base residue E160A, in complex with the chromogenic substrate molecule 2,5-dinitrophenyl-beta-D-xyloside. Surprisingly, six of the eight active sites present in the crystallographic asymmetric unit contain the trapped covalent glycosyl-enzyme intermediate, while two of them still contain the uncleaved substrate. The structural characterization of these two critical species along the reaction coordinate of this enzyme identifies the residues forming its xyloside-binding pocket as well as those essential for its aglycone recognition.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16212978}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16212978 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16212978}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| [[Category: Thermophilic enzyme]] | | [[Category: Thermophilic enzyme]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:43:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:38:56 2008'' |
