3u37

Publication Abstract from PubMed

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 fibre-degrading enzymes. We have determined the three-dimensional structure of Est2A, an acetyl xylan esterase from B. proteoclasticus, at 2.1 A resolution, along with the structure of an inactive mutant (H351A) at 2.0 A 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 fibre-degrading enzymes produced by B. proteoclasticus provides a rich source of new enzymes of potential use in industrial settings. Proteins 2013. (c) 2013 Wiley Periodicals, Inc.

Structure and function of an acetyl xylan esterase (est2a) from the rumen bacterium Butyrivibrio proteoclasticus.,Till M, Goldstone DC, Attwood GT, Moon CD, Kelly WJ, Arcus VL Proteins. 2013 Jan 23. doi: 10.1002/prot.24254. PMID:23345031^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.