PDBsum entry: 1r77

Hydrolase

PDB id: 1r77

Contents

Protein chains

99 a.a. *

Waters ×221

* Residue conservation analysis

PDB id:

1r77

Name:

Hydrolase

Title:

Crystal structure of the cell wall targeting domain of peptidylglycan hydrolase ale-1

Structure:

Cell wall targeting domain of glycylglycine endopeptidase ale-1. Chain: a, b. Fragment: cell wall targeting domain. Engineered: yes. Mutation: yes

Source:

Staphylococcus capitis. Organism_taxid: 29388. Strain: epk1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.75Å R-factor: 0.202 R-free: 0.232

Authors:

J.Z.Lu,T.Fujiwara,H.Komatsuzawa,M.Sugai,J.Sakon

Key ref:

J.Z.Lu et al. (2006). Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges. J Biol Chem, 281, 549-558. PubMed id: 16257954 DOI: 10.1074/jbc.M509691200

Date:

20-Oct-03 Release date: 12-Apr-05

Protein chains

O05156  (ALE1_STACP) -  Glycyl-glycine endopeptidase ALE-1

Seq: 362 a.a.

Struc: 99 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.24.75 - Lysostaphin.
• Reaction: Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.
• Cofactor: Zinc

DOI no: 10.1074/jbc.M509691200

J Biol Chem 281:549-558 (2006)

PubMed id: 16257954

Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges.

J.Z.Lu, T.Fujiwara, H.Komatsuzawa, M.Sugai, J.Sakon.

ABSTRACT

ALE-1, a homologue of lysostaphin, is a peptidoglycan hydrolase that specifically lyses Staphylococcus aureus cell walls by cleaving the pentaglycine linkage between the peptidoglycan chains. Binding of ALE-1 to S. aureus cells through its C-terminal 92 residues, known as the targeting domain, is functionally important for staphylolytic activity. The ALE-1-targeting domain belongs to the SH3b domain family, the prokaryotic counterpart of the eukaryotic SH3 domains. The 1.75 angstroms crystal structure of the targeting domain shows an all-beta fold similar to typical SH3s but with unique features. The structure reveals patches of conserved residues among orthologous targeting domains, forming surface regions that can potentially interact with some common features of the Gram-positive cell wall. ALE-1-targeting domain binding studies employing various bacterial peptidoglycans demonstrate that the length of the interpeptide bridge, as well as the amino acid composition of the peptide, confers the maximum binding of the targeting domain to the staphylococcal peptidoglycan. Truncation of the highly conserved first 9 N-terminal residues results in loss of specificity to S. aureus cell wall-targeting, suggesting that these residues confer specificity to S. aureus cell wall.

Selected figure(s)

Figure 6.
FIGURE 6. Binding of native ALE-1-targeting domain (92AA) and its truncated form (83AA) to various peptidoglycans. Underneath the binding chart is the schematic representation of the structure of the interpeptide bridges of these PGs. Bound protein to PG was detected by an ELISA procedure and normalized against bound native form on 209P cells.

Figure 8.
FIGURE 8. Binding of the targeting domain (92AA) and its mutants to S. aureus 209P peptidoglycan. Bound protein to PG was detected by the ELISA procedure and normalized against wild type.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 549-558) copyright 2006.

Figures were selected by an automated process.