Structure and function of an acetyl xylan esterase (Est2A) from the rumen bacterium Butyrivibrio proteoclasticus |
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| Authors: | David C Goldstone Graeme T Attwood Christina D Moon Willam J Kelly Vickery L Arcus |
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| Institution: | 1. AgResearch Structural Biology Laboratory and School of Biological Sciences, University of Auckland, Auckland, New Zealand;2. AgResearch Grasslands, Palmerston North, New Zealand;3. Department of Biological Sciences, University of Waikato, Hamilton, New Zealand |
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| Abstract: | 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 Å resolution, along with the structure of an inactive mutant (H351A) at 2.0 Å resolution. The structure reveals two domains—a 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. © 2012 Wiley Periodicals, Inc. |
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| Keywords: | acetyl xylan esterase rumen CE2 SGNH domain |
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