5ITW

Crystal structure of Bacillus subtilis BacC Dihydroanticapsin 7-dehydrogenase

5ITW の概要

• エントリーDOI: 10.2210/pdb5itw/pdb
• 関連するPDBエントリー: 5ITV
• 分子名称: Dihydroanticapsin 7-dehydrogenase, SULFATE ION (3 entities in total)
• 機能のキーワード: oxidoreductase, short-chain dehydrogenases/reductases, rossmann fold, nad(p) binding domain
• 由来する生物種: Bacillus subtilis (strain 168)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 110169.68

構造登録者

Perinbam, K.,Balaram, H.,Row, T.N.G.,Gopal, B. (登録日: 2016-03-17, 公開日: 2017-02-22, 最終更新日: 2023-11-08)

主引用文献

Perinbam, K.,Balaram, H.,Guru Row, T.N.,Gopal, B.
Probing the influence of non-covalent contact networks identified by charge density analysis on the oxidoreductase BacC.
Protein Eng. Des. Sel., 30:265-272, 2017

PubMed Abstract: Bacillus subtilis BacC is an oxidoreductase involved in the biosynthesis of the potent antibiotic bacilysin. The crystal structure of BacC was determined at 1.19 Å resolution. An experimental charge density approach was used to calculate non-covalent interactions within the monomer and across the dimeric interface of BacC. This interaction network, in turn, enabled an analysis of non-covalently connected paths that span the protein structure. One of the pathways of non-covalent interactions was examined by mutational analysis. Biochemical analysis of BacC mutants with potential disruptions in non-covalent interactions along this path revealed that residues that form nodes in pathways of non-covalent interactions influence catalytic activity more than others in a similar chemical environment. Furthermore, we note that nodes in the non-covalent interaction networks are co-localized with compensatory mutation sites identified by multiple sequence alignment of proteins with low sequence similarity to BacC. Put together, this analysis supports the hypothesis that non-covalent nodes represent conserved structural features that can impact the catalytic activity of an enzyme.

PubMed: 28158843
DOI: 10.1093/protein/gzx006

実験手法

X-RAY DIFFRACTION (1.19 Å)