5XHB

Crystal structure of the full length of NisI in a lipid free form, the nisin immunity protein, from Lactococcus lactis

Summary for 5XHB

• Entry DOI: 10.2210/pdb5xhb/pdb
• Descriptor: Nisin immunity protein, SULFATE ION (3 entities in total)
• Functional Keywords: immunity protein, immune system
• Biological source: Lactococcus lactis subsp. lactis
• Cellular location: Cell membrane ; Lipid-anchor : P42708
• Total number of polymer chains: 1
• Total formula weight: 26414.65

Authors

Ha, S.C. (deposition date: 2017-04-20, release date: 2017-12-27, Last modification date: 2018-03-07)

Primary citation

Jeong, J.H.,Ha, S.C.
Crystal Structure of NisI in a Lipid-Free Form, the Nisin Immunity Protein, from Lactococcus lactis
Antimicrob. Agents Chemother., 62:-, 2018

PubMed Abstract: Nisin is a lantibiotic, a member of a family of polypeptides containing lanthionine with antimicrobial activity. Nisin-producing microorganisms require immunity proteins for self-protection from nisin itself. , a microorganism that synthesizes nisin, has an integral NisFEG ABC transporter and an NisI lipoprotein that function in nisin immunity. Here, we present the crystal structure of the full length of NisI, a lipid-free form of NisI, determined at 1.9-Å resolution. As with the nuclear magnetic resonance (NMR) structures of the N- and C-terminal domains of NisI, NisI is composed of N- and C-terminal domains, both of which display a fold similar to that found in SpaI, a lipoprotein with immunity against subtilin in The full-length structure of NisI reveals a large, deep cleft by the interdomain association, one side of which is occupied by the residues important for immunity. Opposite the cleft, a shallow groove is found where nisin-interacting residues are distributed in the periphery composed of the C-terminal negative patch. Based on a sulfate ion found in the large and deep cleft, a model of NisI in complex with a farnesyl diphosphate backbone of lipid II is proposed, suggesting a mechanism for increasing the chances of encountering nisin.

PubMed: 29311076
DOI: 10.1128/AAC.01966-17

Experimental method

X-RAY DIFFRACTION (1.9 Å)