Till sidans topp

Sidansvarig: Webbredaktion
Sidan uppdaterades: 2012-09-11 15:12

Tipsa en vän
Utskriftsversion

Nuclear Magnetic Resonanc… - Göteborgs universitet Till startsida
Webbkarta
Till innehåll Läs mer om hur kakor används på gu.se

Nuclear Magnetic Resonance Structure and Mutational Analysis of the Lactococcin A Immunity Protein.

Artikel i vetenskaplig tidskrift
Författare Per Eugen Kristiansen
Cecilia Persson
Virginia Fuochi
Anders Pedersen
B Göran Karlsson
Jon Nissen-Meyer
Camilla Oppegård
Publicerad i Biochemistry
Volym 55
Nummer/häfte 45
Sidor 6250-6257
ISSN 1520-4995
Publiceringsår 2016
Publicerad vid Svenskt NMR-centrum vid Göteborgs universitet
Sidor 6250-6257
Språk en
Länkar doi.org/10.1021/acs.biochem.6b00848
www.ncbi.nlm.nih.gov/entrez/query.f...
Ämneskategorier Strukturbiologi

Sammanfattning

The class IId bacteriocin lactococcin A and the pediocin-like bacteriocins induce membrane leakage and cell death by specifically binding the mannose phophotransferase system (man-PTS) on their target cells. The bacteriocins' cognate immunity proteins that protect the producer cell from its own bacteriocin recognize and bind to the bacteriocin-man-PTS complex and thereby block membrane leakage. In this study, we have determined the three-dimensional structure of the lactococcin A immunity protein (LciA) by the use of nuclear magnetic resonance spectroscopy. LciA forms a four-helix bundle structure with a flexible C-terminal tail. Despite the low degree of sequence similarity between LciA and the pediocin-like immunity proteins, they share the same fold. However, there are certain differences between the structures. The C-terminal helix in LciA is considerably shorter than that observed in the pediocin-like immunity proteins, and the surface potentials of the immunity proteins differ. Truncated variants of LciA in which 6 or 10 of the C-terminal residues were removed yielded a reduced degree of protection, indicating that the unstructured C-terminal tail is important for the functionality of the immunity proteins.

Sidansvarig: Webbredaktion|Sidan uppdaterades: 2012-09-11
Dela:

På Göteborgs universitet använder vi kakor (cookies) för att webbplatsen ska fungera på ett bra sätt för dig. Genom att surfa vidare godkänner du att vi använder kakor.  Vad är kakor?