8WKO

Crystal structure of O-acetylhomoserine sulfhydrylase from Lactobacillus plantarum in the closed form

Summary for 8WKO

• Entry DOI: 10.2210/pdb8wko/pdb
• Descriptor: L-methionine gamma-lyase, SULFATE ION, PROLINE (3 entities in total)
• Functional Keywords: o-acetylhomoserine sulfhydrylase, lyase
• Biological source: Lactiplantibacillus plantarum JDM1
• Total number of polymer chains: 2
• Total formula weight: 97074.82

Authors

Oda, K.,Matoba, Y. (deposition date: 2023-09-28, release date: 2024-02-14, Last modification date: 2024-10-02)

Primary citation

Matoba, Y.,Oda, K.,Wataeda, M.,Kanemori, H.,Matsuo, K.
pH-dependent regulation of an acidophilic O -acetylhomoserine sulfhydrylase from Lactobacillus plantarum.
Appl.Environ.Microbiol., 90:e0011824-e0011824, 2024

PubMed Abstract: Bacteria have two routes for the l-methionine biosynthesis. In one route called the direct sulfuration pathway, acetylated l-homoserine is directly converted into l-homocysteine. The reaction using HS as the second substrate is catalyzed by a pyridoxal 5'-phosphate-dependent enzyme, -acetylhomoserine sulfhydrylase (OAHS). In the present study, we determined the enzymatic functions and the structures of OAHS from (OAHS). The OAHS enzyme exhibited the highest catalytic activity under the weak acidic pH condition. In addition, crystallographic analysis revealed that the enzyme takes two distinct structures, open and closed forms. In the closed form, two acidic residues are sterically clustered. The proximity may cause the electrostatic repulsion, inhibiting the formation of the closed form under the neutral to the basic pH conditions. We concluded that the pH-dependent regulation mechanism using the two acidic residues contributes to the acidophilic feature of the enzyme.

PubMed: 38568076
DOI: 10.1128/aem.00118-24

Experimental method

X-RAY DIFFRACTION (2.91 Å)