1wu4
From Proteopedia
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| - | [[Image:1wu4.gif|left|200px]] | + | [[Image:1wu4.gif|left|200px]] |
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| - | '''Crystal structure of reducing-end-xylose releasing exo-oligoxylanase''' | + | {{Structure |
| + | |PDB= 1wu4 |SIZE=350|CAPTION= <scene name='initialview01'>1wu4</scene>, resolution 1.35Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Oligosaccharide_reducing-end_xylanase Oligosaccharide reducing-end xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.156 3.2.1.156] | ||
| + | |GENE= BH2105 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2 Bacteria]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of reducing-end-xylose releasing exo-oligoxylanase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WU4 is a [ | + | 1WU4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WU4 OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125., Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shoun H, Kitaoka M, J Biol Chem. 2005 Apr 29;280(17):17180-6. Epub 2005 Feb 17. PMID:[http:// | + | Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125., Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shoun H, Kitaoka M, J Biol Chem. 2005 Apr 29;280(17):17180-6. Epub 2005 Feb 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15718242 15718242] |
[[Category: Bacteria]] | [[Category: Bacteria]] | ||
[[Category: Oligosaccharide reducing-end xylanase]] | [[Category: Oligosaccharide reducing-end xylanase]] | ||
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[[Category: glycoside hydrolase family 8]] | [[Category: glycoside hydrolase family 8]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:01:33 2008'' |
Revision as of 13:01, 20 March 2008
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| , resolution 1.35Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | BH2105 (Bacteria) | ||||||
| Activity: | Oligosaccharide reducing-end xylanase, with EC number 3.2.1.156 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of reducing-end-xylose releasing exo-oligoxylanase
Overview
Reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125 (Rex) hydrolyzes xylooligosaccharides whose degree of polymerization is greater than or equal to 3, releasing the xylose unit at the reducing end. It is a unique exo-type glycoside hydrolase that recognizes the xylose unit at the reducing end in a very strict manner, even discriminating the beta-anomeric hydroxyl configuration from the alpha-anomer or 1-deoxyxylose. We have determined the crystal structures of Rex in unliganded and complex forms at 1.35-2.20-A resolution and revealed the structural aspects of its three subsites ranging from -2 to +1. The structure of Rex was compared with those of endo-type enzymes in glycoside hydrolase subfamily 8a (GH-8a). The catalytic machinery of Rex is basically conserved with other GH-8a enzymes. However, subsite +2 is blocked by a barrier formed by a kink in the loop before helix alpha10. His-319 in this loop forms a direct hydrogen bond with the beta-hydroxyl of xylose at subsite +1, contributing to the specific recognition of anomers at the reducing end.
About this Structure
1WU4 is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
Reference
Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125., Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shoun H, Kitaoka M, J Biol Chem. 2005 Apr 29;280(17):17180-6. Epub 2005 Feb 17. PMID:15718242
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