1HCX

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

Summary for 1HCX

• Entry DOI: 10.2210/pdb1hcx/pdb
• Related: 1H8G
• Descriptor: MAJOR AUTOLYSIN, 2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride, CHOLINE ION, ... (5 entities in total)
• Functional Keywords: choline-binding domain, cell wall attachment
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 2
• Total formula weight: 31286.46

Authors

Fernandez-Tornero, C.,Lopez, R.,Garcia, E.,Gimenez-Gallego, G.,Romero, A. (deposition date: 2001-05-10, release date: 2001-11-29, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)