The thermostabilizing domain, XynA, of Caldibacillus cellulovorans xylanase is a xylan binding domain.
We show that the N-terminal 'thermostabilizing domain' (TSD) of the xylanase, XynA, from the thermophilic bacterium Caldibacillus cellulovorans also acts as a xylan binding domain. Affinity electrophoresis experiments show that this TSD selectively binds soluble xylan and binds weakly to hydroxyethylcellulose. Based on this, and previously reported evidence, we propose that xylanase-associated TSDs are xylan binding domains.
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Department of Biological Sciences, Macquarie University, Sydney, NSW 2109, Australia.
Gibbs
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Bergquist
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D000595:Amino Acid Sequence; D001483:Base Sequence; D003013:Clostridium / Q000201:enzymology*; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D043364:Endo-1,4-beta Xylanases; D008969:Molecular Sequence Data; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D014990:Xylans / Q000378:metabolism*; D014995:Xylosidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D017931:DNA Primers; D014990:Xylans; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases