3wn2: Difference between revisions
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{{STRUCTURE_3wn2| PDB=3wn2 | SCENE= }} | |||
===Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with xylohexaose=== | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/EABF_STRCO EABF_STRCO]] Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose), it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well (By similarity). | |||
==About this Structure== | |||
[[3wn2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WN2 OCA]. | |||
[[Category: Non-reducing end alpha-L-arabinofuranosidase]] | |||
[[Category: Fujimoto, Z.]] | |||
[[Category: Harazono, K.]] | |||
[[Category: Ichinose, H.]] | |||
[[Category: Kaneko, S.]] | |||
[[Category: Maehara, T.]] | |||
[[Category: Michikawa, M.]] | |||
[[Category: Five-bladed beta-propeller]] | |||
[[Category: Glycoside hydrolase]] | |||
[[Category: Hydrolase]] | |||
Revision as of 11:28, 5 February 2014
Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with xylohexaose
Function
[EABF_STRCO] Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose), it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well (By similarity).
About this Structure
3wn2 is a 1 chain structure. Full crystallographic information is available from OCA.
