 |
PDBsum entry 5fmw
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Structural protein
|
PDB id
|
|
|
|
5fmw
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of the poly-C9 component of the complement membrane attack complex.
|
|
|
Authors
|
|
N.V.Dudkina,
B.A.Spicer,
C.F.Reboul,
P.J.Conroy,
N.Lukoyanova,
H.Elmlund,
R.H.Law,
S.M.Ekkel,
S.C.Kondos,
R.J.Goode,
G.Ramm,
J.C.Whisstock,
H.R.Saibil,
M.A.Dunstone.
|
|
|
Ref.
|
|
Nat Commun, 2016,
7,
10588.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The membrane attack complex (MAC)/perforin-like protein complement component 9
(C9) is the major component of the MAC, a multi-protein complex that forms pores
in the membrane of target pathogens. In contrast to homologous proteins such as
perforin and the cholesterol-dependent cytolysins (CDCs), all of which require
the membrane for oligomerisation, C9 assembles directly onto the nascent MAC
from solution. However, the molecular mechanism of MAC assembly remains to be
understood. Here we present the 8 Å cryo-EM structure of a soluble form of
the poly-C9 component of the MAC. These data reveal a 22-fold symmetrical
arrangement of C9 molecules that yield an 88-strand pore-forming β-barrel. The
N-terminal thrombospondin-1 (TSP1) domain forms an unexpectedly extensive part
of the oligomerisation interface, thus likely facilitating solution-based
assembly. These TSP1 interactions may also explain how additional C9 subunits
can be recruited to the growing MAC subsequent to membrane insertion.
|
|
|
|
|
|
|
|
Headers
|
|
|
|
|
|
