2ZRR

Crystal structure of an immunity protein that contributes to the self-protection of bacteriocin-producing Enterococcus mundtii 15-1A

Summary for 2ZRR

• Entry DOI: 10.2210/pdb2zrr/pdb
• Descriptor: Mundticin KS immunity protein (2 entities in total)
• Functional Keywords: antiparallel four-helix bundle, antimicrobial protein
• Biological source: Enterococcus mundtii
• Total number of polymer chains: 1
• Total formula weight: 13290.21

Authors

Jeon, H.J.,Noda, M.,Matoba, Y.,Kumagai, T.,Sugiyama, M. (deposition date: 2008-08-30, release date: 2009-02-17, Last modification date: 2024-03-13)

Primary citation

Jeon, H.J.,Noda, M.,Matoba, Y.,Kumagai, T.,Sugiyama, M.
Crystal structure and mutagenic analysis of a bacteriocin immunity protein, Mun-im
Biochem.Biophys.Res.Commun., 378:574-578, 2009

PubMed Abstract: Bacteriocin-producing lactic acid bacteria (LAB) possess a self-protection factor, which is generally called an immunity protein. In this study, we determine the crystal structure of an immunity protein, designated Mun-im, which was classified into subgroup B immunity proteins for class IIa bacteriocins. The Mun-im protein takes a left-turning antiparallel four-helix bundle structure with the flexible N- and C-terminal parts. Although the amino acid sequences of the subgroup B immunity proteins are distinguished from those of the subgroup A, the core structure of Mun-im is well-superimposed with that of the subgroup A immunity protein, EntA-im, and the C-terminus of both proteins is flexible. However, the C-terminus of Mun-im is obviously shorter than that of the subgroup A. We found through mutagenic study of Mun-im that the C-terminus and the K86 residue on the helix 4 in the immunity protein molecule are important for expression of the immunity activity on the subgroup B immunity proteins.

PubMed: 19061861
DOI: 10.1016/j.bbrc.2008.11.093

Experimental method

X-RAY DIFFRACTION (1.8 Å)