2c1g

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2c1g, resolution 1.75Å

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STRUCTURE OF STREPTOCOCCUS PNEUMONIAE PEPTIDOGLYCAN DEACETYLASE (SPPGDA)

Overview

Streptococcus pneumoniae peptidoglycan GlcNAc deacetylase (SpPgdA), protects the Gram-positive bacterial cell wall from host lysozymes by, deacetylating peptidoglycan GlcNAc residues. Deletion of the pgda gene has, been shown to result in hypersensitivity to lysozyme and reduction of, infectivity in a mouse model. SpPgdA is a member of the family 4, carbohydrate esterases, for which little structural information exists, and no catalytic mechanism has yet been defined. Here we describe the, native crystal structure and product complexes of SpPgdA biochemical, characterization and mutagenesis. The structural data show that SpPgdA is, an elongated three-domain protein in the crystal. The structure, in, combination with mutagenesis, shows that SpPgdA is a metalloenzyme using a, His-His-Asp ... [(full description)]

About this Structure

2C1G is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with ACT, ZN and PEG as [ligands]. Active as [N-acetylglucosamine deacetylase], with EC number [3.5.1.33]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor., Blair DE, Schuttelkopf AW, MacRae JI, van Aalten DM, Proc Natl Acad Sci U S A. 2005 Oct 25;102(43):15429-34. Epub 2005 Oct 12. PMID:16221761

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