"A genomic library of Clostridium thermocellum DNA constructed in lambda ZAPII was screened for xylanase-expressing clones. Cross-hybridization experiments revealed a new xylanase gene isolated from the gene library, which was designated xyn Y."

"The encoded enzyme, xylanase Y (XYLY), displayed features characteristic of an endo-beta1,4-xylanase: the enzyme rapidly hydrolysed oat spelt, wheat and rye arabinoxylans and was active against methyl-umbelliferyl-beta-D-cellobioside, but did not hydrolyse any cellulosic substrates."

"The encoded enzyme contained a typical N-terminal 26-residue signal peptide, followed by a 164 amino acid sequence, designated domain A, that was not essential for catalytic activity."

"Western blot analysis using antiserum raised against XYLY showed that the xylanase was located in the cellulosome and did not appear to be extensively glycosylated."

"The pH and temperature optima of the enzyme were 6.8 and 75 degrees C respectively"

"Here we report the structure of the cohesin-dockerin complex from Clostridium thermocellum at 2.2-A resolution."

"The data show that the beta-sheet cohesin domain interacts predominantly with one of the helices of the dockerin."

"the classical 12-residue EF-hand coordination to two calcium ions is maintained."

"internal sequence duplication within the dockerin is manifested in near-perfect internal twofold symmetry"

"The dual binding mode is predicted to impart significant plasticity into the orientation of the catalytic subunits within this supramolecular assembly"

"The sequence duplication is reflected in near-perfect 2-fold structural symmetry, suggesting that both repeats could interact with cohesins by a common mechanism"

"The dual binding mode is predicted to impart significant plasticity into the orientation of the catalytic subunits within this supramolecular assembly"