2bfg
From Proteopedia
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| - | [[Image:2bfg.gif|left|200px]]<br /><applet load="2bfg" size=" | + | [[Image:2bfg.gif|left|200px]]<br /><applet load="2bfg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bfg, resolution 2.40Å" /> | caption="2bfg, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF BETA-XYLOSIDASE (FAM GH39) IN COMPLEX WITH DINITROPHENYL-BETA-XYLOSIDE AND COVALENTLY BOUND XYLOSIDE'''<br /> | '''CRYSTAL STRUCTURE OF BETA-XYLOSIDASE (FAM GH39) IN COMPLEX WITH DINITROPHENYL-BETA-XYLOSIDE AND COVALENTLY BOUND XYLOSIDE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with XYS, NA, SO4 and ANX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xylan_1,4-beta-xylosidase Xylan 1,4-beta-xylosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.37 3.2.1.37] Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain H'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=XYS:'>XYS</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ANX:'>ANX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xylan_1,4-beta-xylosidase Xylan 1,4-beta-xylosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.37 3.2.1.37] Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+H'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thermophilic enzyme]] | [[Category: thermophilic enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:23:28 2008'' |
Revision as of 08:23, 3 February 2008
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CRYSTAL STRUCTURE OF BETA-XYLOSIDASE (FAM GH39) IN COMPLEX WITH DINITROPHENYL-BETA-XYLOSIDE AND COVALENTLY BOUND XYLOSIDE
Overview
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.
About this Structure
2BFG is a Single protein structure of sequence from Geobacillus stearothermophilus with , , and as ligands. Active as Xylan 1,4-beta-xylosidase, with EC number 3.2.1.37 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Enzyme-substrate complex structures of a GH39 beta-xylosidase from Geobacillus stearothermophilus., Czjzek M, Ben David A, Bravman T, Shoham G, Henrissat B, Shoham Y, J Mol Biol. 2005 Nov 4;353(4):838-46. Epub 2005 Sep 20. PMID:16212978
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