Structure and function of an acetyl xylan esterase (Est2A) from the rumen bacterium Butyrivibrio proteoclasticus

作者:Till Marisa; Goldstone David C; Attwood Graeme T; Moon Christina D; Kelly Willam J; Arcus Vickery L*
来源:Proteins: Structure, Function, and Genetics , 2013, 81(5): 911-917.
DOI:10.1002/prot.24254

摘要

Butyrivibrio proteoclasticus is a significant component of the microbial population of the rumen of dairy cattle. It is a xylan-degrading organism whose genome encodes a large number of open reading frames annotated as fiber-degrading enzymes. We have determined the three-dimensional structure of Est2A, an acetyl xylan esterase from B. proteoclasticus, at 2.1 angstrom resolution, along with the structure of an inactive mutant (H351A) at 2.0 angstrom resolution. The structure reveals two domainsa C-terminal SGNH domain and an N-terminal jelly-roll domain typical of CE2 family structures. The structures are accompanied by experimentally determined enzymatic parameters against two model substrates, para-nitrophenyl acetate and para-nitrophenyl butyrate. The suite of fiber-degrading enzymes produced by B. proteoclasticus provides a rich source of new enzymes of potential use in industrial settings. Proteins 2013.

  • 出版日期2013-5