4DEV
An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus.
Summary for 4DEV
| Entry DOI | 10.2210/pdb4dev/pdb |
| Related | 3U37 |
| Descriptor | Acetyl-xylan esterase Est2A, ACETIC ACID, DI(HYDROXYETHYL)ETHER, ... (6 entities in total) |
| Functional Keywords | acetyl xylan esterase, hydrolase |
| Biological source | Butyrivibrio proteoclasticus |
| Total number of polymer chains | 8 |
| Total formula weight | 371697.83 |
| Authors | Till, M.,Arcus, V.L. (deposition date: 2012-01-22, 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 Cited by 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: 23345031DOI: 10.1002/prot.24254 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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