PDBsum entry 2ls0

Hydrolase

PDB id: 2ls0

Contents

Protein chain

128 a.a.

PDB id:

2ls0

Name:

Hydrolase

Title:

Solution structure of the target recognition domain of zoocin a

Structure:

Zoocin a endopeptidase. Chain: 1. Fragment: unp residues 170-285. Engineered: yes

Source:

Streptococcus equi subsp. Zooepidemicus. Organism_taxid: 40041. Gene: zooa. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

R.Timkovich,Y.Chen,R.S.Simmonds

Key ref:

Y.Chen et al. (2013). Solution structure of the recombinant target recognition domain of zoocin A. Proteins, 81, 722-727. PubMed id: 23184858 DOI: 10.1002/prot.24224

Date:

17-Apr-12 Release date: 05-Dec-12

Protein chain

O54308  (O54308_STRSZ) -  Peptidase, M23/M37 family from Streptococcus equi subsp. zooepidemicus

Seq: 285 a.a.

Struc: 128 a.a.*

* PDB and UniProt seqs differ at 12 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: Zn(2+)

DOI no: 10.1002/prot.24224

Proteins 81:722-727 (2013)

PubMed id: 23184858

Solution structure of the recombinant target recognition domain of zoocin A.

Y.Chen, R.S.Simmonds, J.K.Young, R.Timkovich.

ABSTRACT

The protein rTRD is the recombinant form of the target recognition domain of zoocin A, a lytic exoenzyme produced by Streptococcus equi subspecies zooepidemicus 4881. It has no known sequence homologs. However, the catalytic domain of zoocin A is homologous to lysostaphin which is another exoenzyme active against a different spectrum of bacteria, including the pathogen Staphylococcus aureus. An ensemble of models for the solution structure of rTRD has been generated by NMR techniques. The minimum energy model from the ensemble was subjected to three-dimensional homology search engines, but no homologs were found, suggesting rTRD may represent a new protein folding family. There is some similarity in the folding of rTRD to the immunoglobin fold of the antigen binding region of mammalian antibodies which could suggest an ancient evolutionary relation. © Proteins 2013. © 2012 Wiley Periodicals, Inc.