7E43

Structural insights into a bifunctional peptide methionine sulfoxide reductase MsrA/B fusion protein from Helicobacter pylori

Summary for 7E43

• Entry DOI: 10.2210/pdb7e43/pdb
• Descriptor: Peptide methionine sulfoxide reductase MsrA/MsrB, ACETATE ION (3 entities in total)
• Functional Keywords: msrab; fusion protein; linker region, oxidoreductase
• Biological source: Helicobacter pylori 26695
• Total number of polymer chains: 2
• Total formula weight: 82855.65

Authors

Kim, S.,Lee, K.,Hwang, K.Y. (deposition date: 2021-02-10, release date: 2021-04-21, Last modification date: 2023-11-29)

Primary citation

Kim, S.,Lee, K.,Park, S.H.,Kwak, G.H.,Kim, M.S.,Kim, H.Y.,Hwang, K.Y.
Structural Insights into a Bifunctional Peptide Methionine Sulfoxide Reductase MsrA/B Fusion Protein from Helicobacter pylori .
Antioxidants (Basel), 10:-, 2021

PubMed Abstract: Methionine sulfoxide reductase (Msr) is a family of enzymes that reduces oxidized methionine and plays an important role in the survival of bacteria under oxidative stress conditions. MsrA and MsrB exist in a fusion protein form (MsrAB) in some pathogenic bacteria, such as (), , and . To understand the fused form instead of the separated enzyme at the molecular level, we determined the crystal structure of MsrAB at 2.2 Å, which showed that a linker region (, 193-205) between two domains interacted with each MsrA or MsrB domain via three salt bridges (E193-K107, D197-R103, and K200-D339). Two acetate molecules in the active site pocket showed an planar electron density map in the crystal structure, which interacted with the conserved residues in fusion MsrABs from the pathogen. Biochemical and kinetic analyses revealed that is required to increase the catalytic efficiency of MsrAB. Two salt bridge mutants (D193A and E199A) were located at the entrance or tailgate of . Therefore, the linker region of the MsrAB fusion enzyme plays a key role in the structural stability and catalytic efficiency and provides a better understanding of why MsrAB exists in a fused form.

PubMed: 33807684
DOI: 10.3390/antiox10030389

Experimental method

X-RAY DIFFRACTION (2.2 Å)