4L1G

Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus

4L1G の概要

• エントリーDOI: 10.2210/pdb4l1g/pdb
• 分子名称: Peptidoglycan N-acetylglucosamine deacetylase, SULFATE ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: tim barrel, hydrolase, polysaccharide deacetylase
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 126605.78

構造登録者

Tsalafouta, A.,Fadouloglou, V.E.,Kokkinidis, M. (登録日: 2013-06-03, 公開日: 2014-06-04, 最終更新日: 2023-12-06)

主引用文献

Fadouloglou, V.E.,Balomenou, S.,Aivaliotis, M.,Kotsifaki, D.,Arnaouteli, S.,Tomatsidou, A.,Efstathiou, G.,Kountourakis, N.,Miliara, S.,Griniezaki, M.,Tsalafouta, A.,Pergantis, S.A.,Boneca, I.G.,Glykos, N.M.,Bouriotis, V.,Kokkinidis, M.
Unusual alpha-Carbon Hydroxylation of Proline Promotes Active-Site Maturation.
J.Am.Chem.Soc., 139:5330-5337, 2017

PubMed Abstract: The full extent of proline (Pro) hydroxylation has yet to be established, as it is largely unexplored in bacteria. We describe here a so far unknown Pro hydroxylation activity which occurs in active sites of polysaccharide deacetylases (PDAs) from bacterial pathogens, modifying the protein backbone at the C atom of a Pro residue to produce 2-hydroxyproline (2-Hyp). This process modifies with high specificity a conserved Pro, shares with the deacetylation reaction the same active site and one catalytic residue, and utilizes molecular oxygen as source for the hydroxyl group oxygen of 2-Hyp. By providing additional hydrogen-bonding capacity, the Pro→2-Hyp conversion alters the active site and enhances significantly deacetylase activity, probably by creating a more favorable environment for transition-state stabilization. Our results classify this process as an active-site "maturation", which is highly atypical in being a protein backbone-modifying activity, rather than a side-chain-modifying one.

PubMed: 28333455
DOI: 10.1021/jacs.6b12209

実験手法

X-RAY DIFFRACTION (2.336 Å)