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3.2.1.136: glucuronoarabinoxylan endo-1,4-beta-xylanase

This is an abbreviated version!
For detailed information about glucuronoarabinoxylan endo-1,4-beta-xylanase, go to the full flat file.

Word Map on EC 3.2.1.136

Reaction

alpha-D-glucopyranuronosyl-(1-2)-[alpha-D-glucopyranuronosyl-(1-2)-[beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)]-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)]-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
+
H2O
=
4-O-beta-D-xylopyranosyl-beta-D-xylopyranose
+
alpha-D-glucopyranuronosyl-(1-2)-[alpha-D-glucopyranuronosyl-(1-2)-[beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)]-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta--D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)]-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose

Synonyms

1,4-beta-D-xylan xylanohydrolase, Agu115A, beta-1,4-endoxylanase, bifunctional cellulase/xylanase, endo-beta-xylanase, endoarabinoxylanase, endoglucanase, endoxylanase, feraxan endoxylanase, feraxanase, GH11 endoxylanase, GH115 alpha-glucuronidase, GH30 endoxylanase C, GH30 xylanase, glucuronoxylan xylanohydrolase, glucuronoxylan xylohydrolase, glucuronoxylan-specific xylanase A, glucuronoxylan-specific Xyn30D, glucuronoxylanase, glucuronoxylanase GH30, GuXN 30, M2, M4, TLX, Tx-Xyl, xylanase 30 A, xylanase C, xylanase, glucuronoarabinoxylan endo-1,4-beta-, Xyn30A, Xyn30D, XynA, XynC, XynGH30

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.136 glucuronoarabinoxylan endo-1,4-beta-xylanase

Crystallization

Crystallization on EC 3.2.1.136 - glucuronoarabinoxylan endo-1,4-beta-xylanase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of structure. The protein displays a jelly roll beta-sandwich fold presenting two potential carbohydrate binding clefts, A and B. The cleft A, is located between two loops connecting b4-b5 and b8-b9 strands. Tyr28 and Phe84 present on these loops make a planar hydrophobic binding surface to accommodate sugar ring of ligand. The cleft B, is located on concave surface of beta-sandwich fold. Tyr34 and Tyr104 make a planar hydrophobic platform, which may be inaccessible to ligand due to hindrance by Pro68
purified recombinant His-tagged XynC, 5 mg/ml protein in 20 mM HEPES, 150 mM NaCl pH 7.2, is mixed with 0.2 M sodium tartrate and 20% PEG 3350, which results in a crystal-positive condition with 0.1 M sodium malonate pH 7.0, X-ray diffraction structure determination and analysis at 1.64-2.7 A resolution, molecular replacement
in complex with 4-O-methylaldotetrauronic acid or glucuronate, hanging drop vapor diffusion method, using 200 mM sodium tartrate and 200 mM sodium malonate (pH 7.0) in 19% (w/v) polyethylene glycol 3350
in complex with beta-D-xylopyranosyl-(1->4)-[4-O-methyl-alpha-D-glucuronosyl-(1->2)]-beta-D-xylopyranosyl-(1->4)-D-xylose,hanging drop vapor diffusion method, using 0.1 M imidazole/D,L-malic acid buffer (pH 7.5) and 20% (w/v) poly(ethylene glycol) 1500
purified recombinant catalytic domain GH30 or extended domain CBM35, free or in complex with glucuronic acid, crystallization by mixing of 0.001 ml of 22 mg/ml protein in 20 mM Tris, pH 8.0, and 150 mM NaCl with 0.001 ml of a solution containing 20% w/v PEG 6000, 0.2 M Ca2Cl, and either 0.1 M MES, pH 6.0, or 0.1 M Hepes, pH 7.0, and equilibration by vapor diffusion at room temperature, complexes are obtained by the soaking technique using glucuronic acid or a mixture of aldotriouronic, aldotetraouronic, and aldopentaouronic acids, in a ratio of 2:2:1, cryoprotection by 20% v/v glycerol, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement, modelling