2ZYC

Crystal structure of peptidoglycan hydrolase from Sphingomonas sp. A1

Summary for 2ZYC

• Entry DOI: 10.2210/pdb2zyc/pdb
• Descriptor: Peptidoglycan hydrolase FlgJ, PHOSPHATE ION (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Sphingomonas sp. A1
• Total number of polymer chains: 1
• Total formula weight: 18822.77

Authors

Ochiai, A.,Mikami, B.,Hashimoto, W.,Murata, K. (deposition date: 2009-01-19, release date: 2009-02-03, Last modification date: 2024-05-29)

Primary citation

Hashimoto, W.,Ochiai, A.,Momma, K.,Itoh, T.,Mikami, B.,Maruyama, Y.,Murata, K.
Crystal structure of the glycosidase family 73 peptidoglycan hydrolase FlgJ
Biochem.Biophys.Res.Commun., 381:16-21, 2009

PubMed 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.

PubMed: 19351587
DOI: 10.1016/j.bbrc.2009.01.186

Experimental method

X-RAY DIFFRACTION (1.74 Å)