5C0Q

Crystal structure of Zn bound CbsA from Thermotoga neapolitana

5C0Q の概要

• エントリーDOI: 10.2210/pdb5c0q/pdb
• 関連するPDBエントリー: 5BZA
• 分子名称: Beta-N-acetylhexosaminidase, ZINC ION (2 entities in total)
• 機能のキーワード: cbsa, thermotoga, thermostable enzyme, beta-n-acetylglucosaminidase, hydrolase
• 由来する生物種: Thermotoga neapolitana
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 212838.54

構造登録者

Ha, N.C.,Kim, J.S.,Yoon, B.Y. (登録日: 2015-06-12, 公開日: 2015-09-16, 最終更新日: 2024-10-30)

主引用文献

Kim, J.S.,Yoon, B.Y.,Ahn, J.,Cha, J.,Ha, N.C.
Crystal structure of beta-N-acetylglucosaminidase CbsA from Thermotoga neapolitana
Biochem.Biophys.Res.Commun., 464:869-874, 2015

PubMed Abstract: CbsA from the thermophilic marine bacteria Thermotoga neapolitana is a chitinolyitc enzyme that can cleave a glycosidic bond of the polymer N-acetylglucosamine at the non-reducing end. This enzyme has particularly high activity on di-N-acetylchitobiose. CbsA consists of a family of 3 glycoside hydrolase (GH3)-type catalytic domains and a unique C-terminal domain. The C-terminal domain distinguishes CbsA from other GH3-type enzymes. Sequence analyses have suggested that CbsA has the Asp-His dyad as a general acid/base with the NagZ of Bacillus subtilis and the Salmonella enterica serovar Typhimurium. Here, we determined the crystal structure of CbsA from T. neapolitana at a resolution of 2.0 Å using the Zn-SAD method, revealing a unique homodimeric assembly facilitated by the C-terminal domains in the dimer. We observed that CbsA is strongly inhibited by ZnCl2, and two zinc ions were consistently bound in the active site. Our results can explain the zinc ion's inhibition mechanism in the subfamily of GH3 enzymes, and provide information on the structural diversity and substrate specificity of this hydrolase family.

PubMed: 26187666
DOI: 10.1016/j.bbrc.2015.07.053

実験手法

X-RAY DIFFRACTION (2.499 Å)