1W1A

Structure of Bacillus subtilis PdaA in complex with NAG, a family 4 Carbohydrate esterase.

1W1A の概要

• エントリーDOI: 10.2210/pdb1w1a/pdb
• 関連するPDBエントリー: 1NY1 1W17 1W1B
• 分子名称: PROBABLE POLYSACCHARIDE DEACETYLASE PDAA, CADMIUM ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: family 4 carbohydrate esterase, deacetylase, peptidoglycan, nodb homology domain, hydrolase, sporulation
• 由来する生物種: BACILLUS SUBTILIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59439.66

構造登録者

Blair, D.E.,van Aalten, D.M.F. (登録日: 2004-06-18, 公開日: 2005-01-10, 最終更新日: 2024-05-08)

主引用文献

Blair, D.E.,van Aalten, D.M.
Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine.
FEBS Lett., 570:13-19, 2004

PubMed Abstract: Family 4 carbohydrate esterases deacetylate polymeric carbohydrate substrates such as chitin, acetyl xylan and peptidoglycan. Although some of these enzymes have recently been enzymologically characterised, neither their structure nor their reaction mechanism has been defined. Sequence conservation in this family has pointed to a conserved core, termed the NodB homology domain. We describe the cloning, purification and 1.9 A crystal structure of PdaA, a peptidoglycan deacetylase from Bacillus subtilis. The enzyme assumes a fold related to a (beta/alpha)8 barrel, with a long groove on the surface of the protein that harbours all conserved residues. A complex with the substrate analogue N-acetyl-glucosamine was refined to 2.25 A resolution, revealing interactions of an aspartic acid and three histidines, all conserved in the NodB homology domain, with the ligand. The PdaA structure provides a template for interpreting the wealth of sequence data on family 4 carbohydrate esterases in a structural context and represents a first step towards understanding the reaction mechanism of this family of enzymes.

PubMed: 15251431
DOI: 10.1016/j.febslet.2004.06.013

実験手法

X-RAY DIFFRACTION (2.25 Å)