3E0O

Crystal structure of MsrB

Summary for 3E0O

• Entry DOI: 10.2210/pdb3e0o/pdb
• Related: 3E0M
• Descriptor: Peptide methionine sulfoxide reductase msrB (2 entities in total)
• Functional Keywords: msrb, oxidoreductase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 6
• Total formula weight: 100546.39

Authors

Park, A.K.,Shin, Y.J.,Kim, Y.K.,Chi, Y.M.,Hwang, K.Y. (deposition date: 2008-07-31, release date: 2009-06-16, Last modification date: 2024-03-20)

Primary citation

Kim, Y.K.,Shin, Y.J.,Lee, W.-H.,Kim, H.-Y.,Hwang, K.Y.
Structural and Kinetic Analysis of an MsrA-MsrB Fusion Protein from Streptococcus pneumoniae
Mol.Microbiol., 72:699-709, 2009

PubMed Abstract: Methionine sulphoxide reductases (Msr) catalyse the reduction of oxidized methionine to methionine. These enzymes are divided into two classes, MsrA and MsrB, according to substrate specificity. Although most MsrA and MsrB exist as separate enzymes, in some bacteria these two enzymes are fused to form a single polypeptide (MsrAB). Here, we report the first crystal structure of MsrAB from Streptococcus pneumoniae (SpMsrAB) at 2.4 A resolution. SpMsrAB consists of an N-terminal MsrA domain, a C-terminal MsrB domain and a linker. The linker is composed of 13 residues and contains one 3(10)-helix and several hydrogen bonds interacting with both MsrA and MsrB domains. Interestingly, our structure includes the MsrB domain complexed with an SHMAEI hexa-peptide that is the N-terminal region of neighbouring MsrA domain. A kinetic analysis showed that the apparent K(m) of SpMsrAB for the R-form-substrate was 20-fold lower than that for the S-form substrate, indicating that the MsrB domain had a much higher affinity for the substrate than the MsrA domain. Our study reveals the first structure of the MsrAB by providing insights into the formation of a disulphide bridge in the MsrB, the structure of the linker region, and the distinct structural nature of active site of each MsrA and MsrB domain.

PubMed: 19400786
DOI: 10.1111/j.1365-2958.2009.06680.x

Experimental method

X-RAY DIFFRACTION (2.6 Å)