1GVM

CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE

1GVM の概要

• エントリーDOI: 10.2210/pdb1gvm/pdb
• 関連するPDBエントリー: 1H8G 1HCX
• 分子名称: AUTOLYSIN, CHOLINE ION, DECYLAMINE-N,N-DIMETHYL-N-OXIDE, ... (5 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 (PNEUMOCOCCUS)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 97666.74

構造登録者

Fernandez-Tornero, C.,Lopez, R.,Garcia, E.,Gimenez-Gallego, G.,Romero, A. (登録日: 2002-02-15, 公開日: 2002-08-01, 最終更新日: 2023-12-13)

主引用文献

Fernandez-Tornero, C.,Garcia, E.,Lopez, R.,Gimenez-Gallego, G.,Romero, A.
Two New Crystal Forms of the Choline-Binding Domain of the Major Pneumococcal Autolysin: Insights Into the Dynamics of the Active Dimeric
J.Mol.Biol., 321:163-, 2002

PubMed Abstract: Very little is known about the in vivo regulation of the catalytic activity of the major pneumococcal autolysin (LytA), a surface-exposed enzyme that rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone. Two new crystal forms of the cell wall anchoring domain of LytA were obtained, and their structures were solved and refined to 2.4A and 2.8A resolution. The domain is a homodimer with a boomerang-like shape in which the tertiary structure of each monomer is comprised by six independent beta hairpins arranged in a superhelical fashion. Choline molecules at the hydrophobic interface of consecutive hairpins maintain this unique structure. The C-terminal hairpin (last 13 residues of LytA) in the solenoid is responsible for the formation of the catalytically active homodimer. Although the general fold in the structures derived from both crystal forms is essentially the same, two different conformations of the basic homodimer are observed. Biochemical approaches have demonstrated the fundamental role of the 11 C-terminal residues in the catalytic activity of LytA. The studies reported here reveal the importance of some amino acid residues at the C terminus in the determination of the relative distance of the active dimeric form of the autolysin, which appears to be essential for the catalytic activity of this enzyme.

PubMed: 12139941
DOI: 10.1016/S0022-2836(02)00596-X

実験手法

X-RAY DIFFRACTION (2.8 Å)