3OS6

Crystal structure of putative 2,3-dihydroxybenzoate-specific isochorismate synthase, DhbC from Bacillus anthracis.

3OS6 の概要

• エントリーDOI: 10.2210/pdb3os6/pdb
• 分子名称: Isochorismate synthase DhbC, SULFATE ION, POLYETHYLENE GLYCOL (N=34), ... (5 entities in total)
• 機能のキーワード: structural genomics, center for structural genomics of infectious diseases, csgid, isochorismate synthase dhbc, isomerase
• 由来する生物種: Bacillus anthracis (anthrax,anthrax bacterium)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 186280.77

構造登録者

Domagalski, M.J.,Chruszcz, M.,Skarina, T.,Onopriyenko, O.,Cymborowski, M.,Savchenko, A.,Edwards, A.,Anderson, W.,Minor, W.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2010-09-08, 公開日: 2010-10-20, 最終更新日: 2024-11-06)

主引用文献

Domagalski, M.J.,Tkaczuk, K.L.,Chruszcz, M.,Skarina, T.,Onopriyenko, O.,Cymborowski, M.,Grabowski, M.,Savchenko, A.,Minor, W.
Structure of isochorismate synthase DhbC from Bacillus anthracis.
Acta Crystallogr.,Sect.F, 69:956-961, 2013

PubMed Abstract: The isochorismate synthase DhbC from Bacillus anthracis is essential for the biosynthesis of the siderophore bacillibactin by this pathogenic bacterium. The structure of the selenomethionine-substituted protein was determined to 2.4 Å resolution using single-wavelength anomalous diffraction. B. anthracis DhbC bears the strongest resemblance to the Escherichia coli isochorismate synthase EntC, which is involved in the biosynthesis of another siderophore, namely enterobactin. Both proteins adopt the characteristic fold of other chorismate-utilizing enzymes, which are involved in the biosynthesis of various products, including siderophores, menaquinone and tryptophan. The conservation of the active-site residues, as well as their spatial arrangement, suggests that these enzymes share a common Mg(2+)-dependent catalytic mechanism.

PubMed: 23989140
DOI: 10.1107/S1744309113021246

実験手法

X-RAY DIFFRACTION (2.4 Å)