Carbohydrate recognition and lysis by bacterial peptidoglycan hydrolases

TY - JOUR

T1 - Carbohydrate recognition and lysis by bacterial peptidoglycan hydrolases

AU - Alcorlo, Martín

AU - Martínez-Caballero, Siseth

AU - Molina, Rafael

AU - Hermoso, Juan A

N1 - Copyright © 2017 Elsevier Ltd. All rights reserved.

PY - 2017/6/1

Y1 - 2017/6/1

N2 - The major component of bacterial cell wall is peptidoglycan (PG), a complex polymer formed by long glycan chains cross-linked by peptide stems. PG is in constant equilibrium requiring well-orchestrated coordination between synthesis and degradation. The resulting cell-wall fragments can be recycled, act as messengers for bacterial communication, as effector molecules in immune response or as signaling molecules triggering antibiotics resistance. Tailoring and recycling of PG requires the cleavage of different covalent bonds of the PG sacculi by a diverse set of specific enzymes whose activities are strictly regulated. Here, we review the molecular mechanisms that govern PG remodeling focusing on the structural information available for the bacterial lytic enzymes and the mechanisms by which they recognize their substrates.

AB - The major component of bacterial cell wall is peptidoglycan (PG), a complex polymer formed by long glycan chains cross-linked by peptide stems. PG is in constant equilibrium requiring well-orchestrated coordination between synthesis and degradation. The resulting cell-wall fragments can be recycled, act as messengers for bacterial communication, as effector molecules in immune response or as signaling molecules triggering antibiotics resistance. Tailoring and recycling of PG requires the cleavage of different covalent bonds of the PG sacculi by a diverse set of specific enzymes whose activities are strictly regulated. Here, we review the molecular mechanisms that govern PG remodeling focusing on the structural information available for the bacterial lytic enzymes and the mechanisms by which they recognize their substrates.

KW - Animals

KW - Bacteria/enzymology

KW - Carbohydrate Metabolism

KW - Databases, Protein

KW - Humans

KW - N-Acetylmuramoyl-L-alanine Amidase/chemistry

KW - Protein Binding

U2 - 10.1016/j.sbi.2017.01.001

DO - 10.1016/j.sbi.2017.01.001

M3 - Review

C2 - 28109980

SN - 0959-440X

VL - 44

SP - 87

EP - 100

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

ER -