5HOE

Crystal structrue of Est24, a carbohydrate acetylesterase from Sinorhizobium meliloti

Summary for 5HOE

• Entry DOI: 10.2210/pdb5hoe/pdb
• Descriptor: Hydrolase, PHOSPHATE ION, HEXAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: est24, carbohydrate acetylesterase, sinorhizobium meliloti, hydrolase
• Biological source: Rhizobium meliloti (strain 1021) (Ensifer meliloti)
• Total number of polymer chains: 4
• Total formula weight: 100938.83

Authors

Oh, C.,Ryu, B.H.,An, D.R.,Nguyen, D.D.,Yoo, W.,Kim, T.,Ngo, D.T.,Kim, H.S.,Park, J.S.,Kim, K.K.,Kim, T.D. (deposition date: 2016-01-19, release date: 2016-04-27, Last modification date: 2023-11-08)

Primary citation

Oh, C.,Ryu, B.H.,An, D.R.,Nguyen, D.D.,Yoo, W.,Kim, T.,Ngo, T.D.,Kim, H.S.,Kim, K.K.,Kim, T.D.
Structural and Biochemical Characterization of an Octameric Carbohydrate Acetylesterase from Sinorhizobium meliloti.
Febs Lett., 590:1242-1252, 2016

PubMed Abstract: Carbohydrate acetylesterases, which have a highly specific role among plant-interacting bacterial species, remove the acetyl groups from plant carbohydrates. Here, we determined the crystal structure of Est24, an octameric carbohydrate acetylesterase from Sinorhizobium meliloti, at 1.45 Å resolution and investigated its biochemical properties. The structure of Est24 consisted of five parallel β strands flanked by α helices, which formed an octameric assembly with two distinct interfaces. The deacetylation activity of Est24 and its mutants around the substrate-binding pocket was investigated using several substrates, including glucose pentaacetate and acetyl alginate. Elucidation of the structure-function relationships of Est24 could provide valuable opportunities for biotechnological explorations.

PubMed: 26991446
DOI: 10.1002/1873-3468.12135

Experimental method

X-RAY DIFFRACTION (1.45 Å)