PDBsum entry: 2zyc

Hydrolase

PDB id: 2zyc

Contents

Protein chain

156 a.a. *

Ligands

PO4

Waters ×184

* Residue conservation analysis

PDB id:

2zyc

Name:

Hydrolase

Title:

Crystal structure of peptidoglycan hydrolase from sphingomonas sp. A1

Structure:

Peptidoglycan hydrolase flgj. Chain: a. Fragment: residues 152-313. Engineered: yes. Mutation: yes

Source:

Sphingomonas sp. A1. Organism_taxid: 90322. Gene: flgj. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.74Å R-factor: 0.201 R-free: 0.238

Authors:

A.Ochiai,B.Mikami,W.Hashimoto,K.Murata

Key ref:

W.Hashimoto et al. (2009). Crystal structure of the glycosidase family 73 peptidoglycan hydrolase FlgJ. Biochem Biophys Res Commun, 381, 16-21. PubMed id: 19351587 DOI: 10.1016/j.bbrc.2009.01.186

Date:

19-Jan-09 Release date: 03-Feb-09

Protein chain

B7XH69  (B7XH69_9SPHN) -  Peptidoglycan hydrolase FlgJ

Seq: 313 a.a.

Struc: 156 a.a.*

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

 Gene Ontology (GO) functional annotation 

• Cellular component: flagellin-based flagellum (1 term)
• Biological process: ciliary or flagellar motility (2 terms)
• Biochemical function: amidase activity (2 terms)

DOI no: 10.1016/j.bbrc.2009.01.186

Biochem Biophys Res Commun 381:16-21 (2009)

PubMed id: 19351587

Crystal structure of the glycosidase family 73 peptidoglycan hydrolase FlgJ.

W.Hashimoto, A.Ochiai, K.Momma, T.Itoh, B.Mikami, Y.Maruyama, K.Murata.

ABSTRACT

Glycoside hydrolase (GH) categorized into family 73 plays an important role in degrading bacterial cell wall peptidoglycan. The flagellar protein FlgJ contains N- and C-terminal domains responsible for flagellar rod assembly and peptidoglycan hydrolysis, respectively. A member of family GH-73, the C-terminal domain (SPH1045-C) of FlgJ from Sphingomonas sp. strain A1 was expressed in Escherichia coli, purified, and characterized. SPH1045-C exhibited bacterial cell lytic activity most efficiently at pH 6.0 and 37 degrees C. The X-ray crystallographic structure of SPH1045-C was determined at 1.74 A resolution by single-wavelength anomalous diffraction. The enzyme consists of two lobes, alpha and beta. A deep cleft located between the two lobes can accommodate polymer molecules, suggesting that the active site is located in the cleft. Although SPH1045-C shows a structural homology with family GH-22 and GH-23 lysozymes, the arrangement of the nucleophile/base residue in the active site is specific to each peptidoglycan hydrolase.