PDBsum entry: 1h09

Hydrolase

PDB-id: 1h09

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

338 a.a. *

Waters ×326

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

1h09

Name:

Hydrolase

Title:

Multimodular pneumococcal cell wall endolysin from phage cp-1

Structure:

Lysozyme. Chain: a. Synonym: murein hydrolase, endolysin, muramidase, cp-1 lysin. Engineered: yes

Source:

Bacteriophage cp-1. Organism_taxid: 10747. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:

P15057 (LYS_BPCP1)

Seq:

Struc:

Seq:

339 a.a.

Struc:

338 a.a.

Key:	PfamA domain
Secondary structure	CATH domain

Enzyme class:

E.C.3.2.1.17   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

Resolution:

2.1Å

R-factor:

0.206

R-free:

0.255

Authors:

J.A.Hermoso,B.Monterroso,A.Albert,P.Garcia,M.Menendez, M.Martinez-Ripoll,J.L.Garcia

Key ref:

J.A.Hermoso et al. (2003). Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.. Structure, 11, 1239-1249. [PubMed id: 14527392] [DOI: 10.1016/j.str.2003.09.005]

Date:

12-Jun-02

Release date:

26-Jun-03

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1016/j.str.2003.09.005

Structure 11:1239-1249 (2003)

PubMed id: 14527392

Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.

J.A.Hermoso, B.Monterroso, A.Albert, B.Galán, O.Ahrazem, P.García, M.Martínez-Ripoll, J.L.García, M.Menéndez.

ABSTRACT

Pneumococcal bacteriophage-encoded lysins are modular choline binding proteins that have been shown to act as enzymatic antimicrobial agents (enzybiotics) against streptococcal infections. Here we present the crystal structures of the free and choline bound states of the Cpl-1 lysin, encoded by the pneumococcal phage Cp-1. While the catalytic module displays an irregular (beta/alpha)(5)beta(3) barrel, the cell wall-anchoring module is formed by six similar choline binding repeats (ChBrs), arranged into two different structural regions: a left-handed superhelical domain configuring two choline binding sites, and a beta sheet domain that contributes in bringing together the whole structure. Crystallographic and site-directed mutagenesis studies allow us to propose a general catalytic mechanism for the whole glycoside hydrolase family 25. Our work provides the first complete structure of a member of the large family of choline binding proteins and reveals that ChBrs are versatile elements able to tune the evolution and specificity of the pneumococcal surface proteins.

Selected figure(s)

Figure 1.
Figure 1. Structure of Modular Cpl-1 Endolysin(A) Stereo representation of Cpl-1 structure with domains colored differently. Catalytic N-terminal, green; linker, orange; CI domain, cyan; CII domain, magenta. Choline molecules are drawn in a ball-and-stick representation.(B) Topology diagram of Cpl-1. Domains are color-coded as in (A) with the antiparallel b8 strand of the catalytic module highlighted in orange. In the choline binding model, the different ChBrs (p1-p6) are labeled.(C) Comparison of the amino acid sequence of the ChBrs and the C-terminal tail in Cpl-1. The structural domain, the repeat number, and their corresponding amino acids are shown on the left. Residues in b strand conformation are shadowed in yellow. Conserved amino acids among the repeats appear in black boxes. Its consensus sequence (>=50%) is shown at the bottom. Upper case indicates 100% conservation.

The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 1239-1249) copyright 2003.

Figure was selected by the author.