1wu4
From Proteopedia
(New page: 200px<br /><applet load="1wu4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wu4, resolution 1.35Å" /> '''Crystal structure of...) |
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| - | [[Image:1wu4.gif|left|200px]]<br /><applet load="1wu4" size=" | + | [[Image:1wu4.gif|left|200px]]<br /><applet load="1wu4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wu4, resolution 1.35Å" /> | caption="1wu4, resolution 1.35Å" /> | ||
'''Crystal structure of reducing-end-xylose releasing exo-oligoxylanase'''<br /> | '''Crystal structure of reducing-end-xylose releasing exo-oligoxylanase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans | + | 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== | ==About this Structure== | ||
| - | 1WU4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with NI and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1WU4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WU4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: glycoside hydrolase family 8]] | [[Category: glycoside hydrolase family 8]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:05 2008'' |
Revision as of 13:48, 21 February 2008
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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 with and as ligands. Active as Oligosaccharide reducing-end xylanase, with EC number 3.2.1.156 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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