1H8G

C-terminal domain of the major autolysin (C-LytA) from Streptococcus pneumoniae

1H8G の概要

• エントリーDOI: 10.2210/pdb1h8g/pdb
• 分子名称: MAJOR AUTOLYSIN, CHOLINE ION (3 entities in total)
• 機能のキーワード: choline-binding domain, cell wall attachment
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22932.71

構造登録者

Fernandez-Tornero, C.,Garcia, E.,Lopez, R.,Gimenez-Gallego, G.,Romero, A. (登録日: 2001-02-06, 公開日: 2002-01-31, 最終更新日: 2024-11-13)

主引用文献

Fernandez-Tornero, C.,Lopez, R.,Garcia, E.,Gimenez-Gallego, G.,Romero, A.
A Novel Solenoid Fold in the Cell Wall Anchoring Domain of the Pneumococcal Virulence Factor Lyta
Nat.Struct.Biol., 8:1020-, 2001

PubMed Abstract: Choline binding proteins are virulence determinants present in several Gram-positive bacteria. Because anchorage of these proteins to the cell wall through their choline binding domain is essential for bacterial virulence, their release from the cell surface is considered a powerful target for a weapon against these pathogens. The first crystal structure of a choline binding domain, from the toxin-releasing enzyme pneumococcal major autolysin (LytA), reveals a novel solenoid fold consisting exclusively of beta-hairpins that stack to form a left-handed superhelix. This unique structure is maintained by choline molecules at the hydrophobic interface of consecutive hairpins and may be present in other choline binding proteins that share high homology to the repeated motif of the domain.

PubMed: 11694890
DOI: 10.1038/NSB724

実験手法

X-RAY DIFFRACTION (2.4 Å)