3U37

An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus.

Summary for 3U37

• Entry DOI: 10.2210/pdb3u37/pdb
• Descriptor: Acetyl-xylan esterase Est2A, ACETIC ACID, GLYCEROL, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: Butyrivibrio proteoclasticus B316
• Total number of polymer chains: 8
• Total formula weight: 370763.45

Authors

Till, M.,Arcus, V. (deposition date: 2011-10-05, release date: 2013-02-13, Last modification date: 2024-02-28)

Primary citation

Till, M.,Goldstone, D.C.,Attwood, G.T.,Moon, C.D.,Kelly, W.J.,Arcus, V.L.
Structure and function of an acetyl xylan esterase (Est2A) from the rumen bacterium Butyrivibrio proteoclasticus.
Proteins, 81:911-917, 2013

PubMed 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.

PubMed: 23345031
DOI: 10.1002/prot.24254

Experimental method

X-RAY DIFFRACTION (2.1 Å)