Structural highlights
Function
ALYS_STRPN Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Autolysin strictly depends on the presence of choline-containing cell walls for activity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA.,Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A Nat Struct Biol. 2001 Dec;8(12):1020-4. PMID:11694890[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2001 Dec;8(12):1020-4. PMID:11694890 doi:10.1038/nsb724
