4TX1

The crystal structure of carbohydrate acetylesterase family member from Sinorhizobium meliloti

Summary for 4TX1

Entry DOI	10.2210/pdb4tx1/pdb
Descriptor	Esterase (2 entities in total)
Functional Keywords	sgnh-hydrolase, acetylesterase, sgnh-family, hydrolase
Biological source	Sinorhizobium meliloti 1021 (Ensifer meliloti)
Total number of polymer chains	3
Total formula weight	73054.67
Authors	Kim, K.,Kim, S.S.,Pandian, R.,Ngo, T.D. (deposition date: 2014-07-02, release date: 2014-12-24, Last modification date: 2023-11-08)
Primary citation	Kim, K.,Ryu, B.H.,Kim, S.S.,An, D.R.,Ngo, T.D.,Pandian, R.,Kim, K.K.,Kim, T.D. Structural and biochemical characterization of a carbohydrate acetylesterase from Sinorhizobium meliloti 1021. Febs Lett., 589:117-122, 2015 Cited by PubMed Abstract: In many microorganisms, carbohydrate acetylesterases remove the acetyl groups from various types of carbohydrates. Sm23 from Sinorhizobium meliloti is a putative member of carbohydrate esterase family 3 (CE3) in the CAZy classification system. Here, we determined the crystal structure of Sm23 at 1.75 Å resolution and investigated functional properties using biochemical methods. Furthermore, immobilized Sm23 exhibited improved stability compared with soluble Sm23, which can be used for the design of plant cell wall degrading-systems. PubMed: 25436419 DOI: 10.1016/j.febslet.2014.11.033 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.75 Å)

Structure validation