论文部分内容阅读
β-xylosidases are glycosidase hydrolases that hydrolyze short xylooligosaccharides into xylose units,which contribute to the final breakdown of plant cell-wall hemicelluloses.Here,we determined the three-dimensional structure of a GH39 β-xylosidases CmXynB1 from a marine bacterium Croceicoccus marinus,which is isolated from the East Pacific polymetallic nodule region.The CmXynB1 showed low second structural identity with other known xylosidases,however,shared similar catalytic fold on 3-D structure.Each monomer of CmXynB1 has a canonical(α/β)8-barrel catalytic domain and an auxiliary β-sandwich domain that plays a role in recognizing the substrate.The structure of CmXynB1 might provide new insights into understanding the mechanism-oxfy loβsidase family.