Work

Structural Insights into MltC from Acinetobacter baumannii : Conservation of the Catalytic Residue and Flexibility in Substrate Recognition

Year: 2026

Type: article

Abstract: Lytic transglycosylases (LTs) are key enzymes involved in bacterial peptidoglycan remodeling.Here, we present the crystal structure of MltC from Acinetobacter baumannii (AbMltC), representing the second reported MltC structure after that of Escherichia coli (EcMltC).The AbMltC structure reveals a conserved catalytic residue, E224, equivalent to E217 of EcMltC, which directly participates in glycosidic bond cleavage.Notably, the substratebinding residue R234, corresponding to R227 of EcMltC, is conserved in sequence but exhibits multiple conformations in AbMltC.This conformational heterogeneity suggests structural flexibility in substrate recognition and provides the structural insights consistent with prior hypothesis that R234 (R227 in EcMltC) functions as a molecular ratchet, facilitating processive cleavage.

Source: Journal of Microbiology and Biotechnology

DOI: 10.4014/jmb.2511.11019

Authors: Hyunseok Jang, Chang Min Kim, Hyun Ho Park

Institutions: Chung-Ang University, The University of Texas Southwestern Medical Center

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

Funders: National Research Foundation, Chung-Ang University, National Research Foundation of Korea, Ministry of Science and ICT, South Korea

Awards: G2722238760, G3677610472