1hcx
From Proteopedia
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CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE
Overview
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 ... [(full description)]
About this Structure
1HCX is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with TPT, CHT and DDQ as [ligands]. Active as [N-acetylmuramoyl-L-alanine amidase], with EC number [3.5.1.28]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].
Reference
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
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