Molecular Basis of Dimerization of Lytic Transglycosylase Revealed by the Crystal Structure of MltA from

Overview

Journal IUCrJ

Date 2021 Nov 22

PMID 34804545

Citations 1

Authors

Hyunseok Jang

Hackwon Do

Chang Min Kim

Gi Eob Kim

Jun Hyuck Lee

Hyun Ho Park

Affiliations

Soon will be listed here.

Abstract

Peptidoglycan digestion by murein-degrading enzymes is a critical process in bacterial cell growth and/or cell division. The membrane-bound lytic murein transglycosylase A (MltA) is a murein-degrading enzyme; it catalyzes the cleavage of the β-1,4-glycosidic linkage between -acetylmuramic acid and -acetylglucosamine in peptidoglycans. Although substrate recognition and cleavage by MltA have been examined by previous structural and mutagenesis studies, the overall mechanism of MltA in conjunction with other functionally related molecules on the outer membrane of bacterial cells for peptidoglycan degradation has remained elusive. In this study, the crystal structure of MltA from the virulent human pathogen is characterized and presented. The study indicated that MltA from forms homodimers via an extra domain which is specific to this species. Furthermore, the working mechanism of MltA with various functionally related proteins on the bacterial outer membrane was modeled based on the structural and biochemical analysis.

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