1uhv: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1uhv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacterium_saccharolyticum Thermoanaerobacterium saccharolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UHV FirstGlance]. <br> | <table><tr><td colspan='2'>[[1uhv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacterium_saccharolyticum Thermoanaerobacterium saccharolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UHV FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DFX:1,2-DEOXY-2-FLUORO-XYLOPYRANOSE'>DFX</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DFX:1,2-DEOXY-2-FLUORO-XYLOPYRANOSE'>DFX</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1px8|1px8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1px8|1px8]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uhv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uhv RCSB], [http://www.ebi.ac.uk/pdbsum/1uhv PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uhv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uhv RCSB], [http://www.ebi.ac.uk/pdbsum/1uhv PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/XYNB_THESA XYNB_THESA]] Has hydrolytic activity towards xylopentaose, xylotriose, xylobiose and P-nitrophenyl-beta-D-xylopyranoside, but has no activity toward xylan. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Thermoanaerobacterium saccharolyticum]] | [[Category: Thermoanaerobacterium saccharolyticum]] | ||
[[Category: Xylan 1,4-beta-xylosidase]] | [[Category: Xylan 1,4-beta-xylosidase]] | ||
[[Category: Ahn, H J | [[Category: Ahn, H J]] | ||
[[Category: Berendzen, J | [[Category: Berendzen, J]] | ||
[[Category: Laivenieks, M | [[Category: Laivenieks, M]] | ||
[[Category: Lee, B Il | [[Category: Lee, B Il]] | ||
[[Category: Liong, E C | [[Category: Liong, E C]] | ||
[[Category: Pedelacq, J D | [[Category: Pedelacq, J D]] | ||
[[Category: Suh, S W | [[Category: Suh, S W]] | ||
[[Category: Vieille, C | [[Category: Vieille, C]] | ||
[[Category: Vocadlo, D J | [[Category: Vocadlo, D J]] | ||
[[Category: Withers, S G | [[Category: Withers, S G]] | ||
[[Category: Yang, J K | [[Category: Yang, J K]] | ||
[[Category: Yoon, H J | [[Category: Yoon, H J]] | ||
[[Category: Zeikus, G J | [[Category: Zeikus, G J]] | ||
[[Category: Covalent glycosyl-enzyme intermediate]] | [[Category: Covalent glycosyl-enzyme intermediate]] | ||
[[Category: Family 39 glycoside hydrolase]] | [[Category: Family 39 glycoside hydrolase]] | ||
Revision as of 11:53, 25 December 2014
Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolaseCrystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase
Structural highlights
Function[XYNB_THESA] Has hydrolytic activity towards xylopentaose, xylotriose, xylobiose and P-nitrophenyl-beta-D-xylopyranoside, but has no activity toward xylan. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed1,4-beta-D-Xylan is the major component of plant cell-wall hemicelluloses. beta-D-Xylosidases are involved in the breakdown of xylans into xylose and belong to families 3, 39, 43, 52, and 54 of glycoside hydrolases. Here, we report the first crystal structure of a member of family 39 glycoside hydrolase, i.e. beta-D-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI. This study also represents the first structure of any beta-xylosidase of the above five glycoside hydrolase families. Each monomer of T. saccharolyticum beta-xylosidase comprises three distinct domains; a catalytic domain of the canonical (beta/alpha)(8)-barrel fold, a beta-sandwich domain, and a small alpha-helical domain. We have determined the structure in two forms: D-xylose-bound enzyme and a covalent 2-deoxy-2-fluoro-alpha-D-xylosyl-enzyme intermediate complex, thus providing two snapshots in the reaction pathway. This study provides structural evidence for the proposed double displacement mechanism that involves a covalent intermediate. Furthermore, it reveals possible functional roles for His228 as the auxiliary acid/base and Glu323 as a key residue in substrate recognition. Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase.,Yang JK, Yoon HJ, Ahn HJ, Lee BI, Pedelacq JD, Liong EC, Berendzen J, Laivenieks M, Vieille C, Zeikus GJ, Vocadlo DJ, Withers SG, Suh SW J Mol Biol. 2004 Jan 2;335(1):155-65. PMID:14659747[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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