PDBsum entry: 1oba

Hydrolase

PDB id: 1oba

Contents

Protein chain

338 a.a. *

Ligands

CHT ×2

Waters ×257

* Residue conservation analysis

PDB id:

1oba

Name:

Hydrolase

Title:

Multimodular pneumococcal cell wall endolysin from phage cp-1 complexed with choline

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.

Resolution:

2.45Å R-factor: 0.205 R-free: 0.264

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:

29-Jan-03 Release date: 17-Oct-03

Protein chain

P15057  (LYS_BPCP1) -  Lysozyme

Seq: 339 a.a.

Struc: 338 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.2.1.17 - Lysozyme.
• 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.

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (6 terms)
• Biochemical function: catalytic activity (5 terms)

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.