3V1H

Structure of the H258Y mutant of Phosphatidylinositol-specific phospholipase C from Staphylococcus aureus

3V1H の概要

• エントリーDOI: 10.2210/pdb3v1h/pdb
• 関連するPDBエントリー: 3v16 3v18
• 分子名称: 1-phosphatidylinositol phosphodiesterase, 1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: pi-cation, tim barrel, phospholipase, lyase
• 由来する生物種: Staphylococcus aureus subsp. aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35086.96

構造登録者

Goldstein, R.I.,Cheng, J.,Stec, B.,Roberts, M.F. (登録日: 2011-12-09, 公開日: 2012-04-04, 最終更新日: 2023-09-13)

主引用文献

Goldstein, R.,Cheng, J.,Stec, B.,Roberts, M.F.
Structure of the S. aureus PI-Specific Phospholipase C Reveals Modulation of Active Site Access by a Titratable PI-Cation Latched Loop
Biochemistry, 51:2579-2587, 2012

PubMed Abstract: Staphylococcus aureus secretes a phosphatidylinositol-specific phospholipase C (PI-PLC) as a virulence factor that is unusual in exhibiting higher activity at acidic pH values than other enzymes in this class. We have determined the crystal structure of this enzyme at pH 4.6 and pH 7.5. Under slightly basic conditions, the S. aureus PI-PLC structure closely follows the conformation of other bacterial PI-PLCs. However, when crystallized under acidic conditions, a large section of mobile loop at the αβ-barrel rim in the vicinity of the active site shows ~10 Å shift. This loop displacement at acidic pH is the result of a titratable intramolecular π-cation interaction between His258 and Phe249. This was verified by a structure of the mutant protein H258Y crystallized at pH 4.6, which does not exhibit the large loop shift. The intramolecular π-cation interaction for S. aureus PI-PLC provides an explanation for the activity of the enzyme at acid pH and also suggests how phosphatidylcholine, as a competitor for Phe249, may kinetically activate this enzyme.

PubMed: 22390775
DOI: 10.1021/bi300057q

実験手法

X-RAY DIFFRACTION (1.9 Å)