|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Proc Natl Acad Sci U S A
103:305-310
(2006)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex.
|
|
J.J.Adams,
G.Pal,
Z.Jia,
S.P.Smith.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Bacterial cell-surface attachment of macromolecular complexes maintains the
microorganism in close proximity to extracellular substrates and allows for
optimal uptake of hydrolytic byproducts. The cellulosome is a large multienzyme
complex used by many anaerobic bacteria for the efficient degradation of plant
cell-wall polysaccharides. The mechanism of cellulosome retention to the
bacterial cell surface involves a calcium-mediated protein-protein interaction
between the dockerin (Doc) module from the cellulosomal scaffold and a cohesin
(Coh) module of cell-surface proteins located within the proteoglycan layer.
Here, we report the structure of an ultra-high-affinity (K(a) = 1.44 x 10(10)
M(-1)) complex between type II Doc, together with its neighboring X module from
the cellulosome scaffold of Clostridium thermocellum, and a type II Coh module
associated with the bacterial cell surface. Identification of X module-Doc and X
module-Coh contacts reveal roles for the X module in Doc stability and enhanced
Coh recognition. This extremely tight interaction involves one face of the Coh
and both helices of the Doc and comprises significant hydrophobic character and
a complementary extensive hydrogen-bond network. This structure represents a
unique mechanism for cell-surface attachment in anaerobic bacteria and provides
a rationale for discriminating between type I and type II Coh modules.
|
|
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
|
|
Figure 3.
Fig. 3. Type II Coh-XDoc complex interface contacts. (a)
Ribbon representation of type II Coh, displaying hydrophobic
interface residues as stick models on the molecular-surface
representation of XDoc. (b) Ribbon representation of XDoc,
displaying hydrophobic interface residues as stick models on the
molecular-surface representation of type II Coh. (c) Interface
hydrogen-bond network, with water molecules shown as red X and
hydrogen-bond contacts as yellow dashed lines. Type II Coh, Doc,
and X module are colored blue, green, and magenta, respectively.
Residues depicted as stick models are labeled accordingly.
|
|
Figure 4.
Fig. 4. Interaction surfaces of type I- and type II Coh-Doc
complexes. Ribbon representations of type II Doc (green) (a) on
the molecular surface of the type II Coh (blue) and type I Doc
(red) (e) on the molecular surface of type I Coh (yellow) (21).
Representations in b and f have been rotated clockwise 90°
around the x axis, followed by a 180° clockwise rotation
around the z axis. Electrostatic surface potential
representations of C. thermocellum type II Coh (c), C.
thermocellum type II Doc (d), C. thermocellum type I Coh (21)
(g), and C. thermocellum type I Doc (21) (h). Positive regions
are shown in blue and negative regions in red. Residues
contributing to the hydrophobic surface character of C.
thermocellum type II Coh are labeled accordingly. The location
of Ile-118 on the surface of the type II Doc and the analogous
residue in the type I Doc (Lys-18) are identified. The
electrostatic surface potentials were calculated in GRASP (47)
and are contoured from -14 (red) to +14 (blue). Ca^2+ ions are
shown as orange spheres.
|
|
|
|
| |
Figures were
selected
by an automated process.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
M.Voronov-Goldman,
R.Lamed,
I.Noach,
I.Borovok,
M.Kwiat,
S.Rosenheck,
L.J.Shimon,
E.A.Bayer,
and
F.Frolow
(2011).
Noncellulosomal cohesin from the hyperthermophilic archaeon Archaeoglobus fulgidus.
|
| |
Proteins,
79,
50-60.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
C.M.Fontes,
and
H.J.Gilbert
(2010).
Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates.
|
| |
Annu Rev Biochem,
79,
655-681.
|
|
|
|
|
|
|
J.Xu,
and
J.C.Smith
(2010).
Probing the mechanism of cellulosome attachment to the Clostridium thermocellum cell surface: computer simulation of the Type II cohesin-dockerin complex and its variants.
|
| |
Protein Eng Des Sel,
23,
759-768.
|
|
|
|
|
|
|
A.Valbuena,
J.Oroz,
R.Hervás,
A.M.Vera,
D.Rodríguez,
M.Menéndez,
J.I.Sulkowska,
M.Cieplak,
and
M.Carrión-Vázquez
(2009).
On the remarkable mechanostability of scaffoldins and the mechanical clamp motif.
|
| |
Proc Natl Acad Sci U S A,
106,
13791-13796.
|
|
|
|
|
|
|
B.A.Pinheiro,
H.J.Gilbert,
K.Sakka,
K.Sakka,
V.O.Fernandes,
J.A.Prates,
V.D.Alves,
D.N.Bolam,
L.M.Ferreira,
and
C.M.Fontes
(2009).
Functional insights into the role of novel type I cohesin and dockerin domains from Clostridium thermocellum.
|
| |
Biochem J,
424,
375-384.
|
|
|
|
|
|
|
I.Noach,
O.Alber,
E.A.Bayer,
R.Lamed,
M.Levy-Assaraf,
L.J.Shimon,
and
F.Frolow
(2008).
Crystallization and preliminary X-ray analysis of Acetivibrio cellulolyticus cellulosomal type II cohesin module: two versions having different linker lengths.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
58-61.
|
|
|
|
|
|
|
J.J.Adams,
K.Gregg,
E.A.Bayer,
A.B.Boraston,
and
S.P.Smith
(2008).
Structural basis of Clostridium perfringens toxin complex formation.
|
| |
Proc Natl Acad Sci U S A,
105,
12194-12199.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
K.Bouchemal
(2008).
New challenges for pharmaceutical formulations and drug delivery systems characterization using isothermal titration calorimetry.
|
| |
Drug Discov Today,
13,
960-972.
|
|
|
|
|
|
|
O.Alber,
I.Noach,
R.Lamed,
L.J.Shimon,
E.A.Bayer,
and
F.Frolow
(2008).
Preliminary X-ray characterization of a novel type of anchoring cohesin from the cellulosome of Ruminococcus flavefaciens.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
77-80.
|
|
|
|
|
|
|
R.Haimovitz,
Y.Barak,
E.Morag,
M.Voronov-Goldman,
Y.Shoham,
R.Lamed,
and
E.A.Bayer
(2008).
Cohesin-dockerin microarray: Diverse specificities between two complementary families of interacting protein modules.
|
| |
Proteomics,
8,
968-979.
|
|
|
|
|
|
|
A.L.Carvalho,
F.M.Dias,
T.Nagy,
J.A.Prates,
M.R.Proctor,
N.Smith,
E.A.Bayer,
G.J.Davies,
L.M.Ferreira,
M.J.Romão,
C.M.Fontes,
and
H.J.Gilbert
(2007).
Evidence for a dual binding mode of dockerin modules to cohesins.
|
| |
Proc Natl Acad Sci U S A,
104,
3089-3094.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
H.J.Gilbert
(2007).
Cellulosomes: microbial nanomachines that display plasticity in quaternary structure.
|
| |
Mol Microbiol,
63,
1568-1576.
|
|
|
|
|
|
|
M.T.Rincon,
T.Cepeljnik,
J.C.Martin,
Y.Barak,
R.Lamed,
E.A.Bayer,
and
H.J.Flint
(2007).
A novel cell surface-anchored cellulose-binding protein encoded by the sca gene cluster of Ruminococcus flavefaciens.
|
| |
J Bacteriol,
189,
4774-4783.
|
|
|
|
|
|
|
P.J.Kundrotas,
and
E.Alexov
(2006).
Electrostatic properties of protein-protein complexes.
|
| |
Biophys J,
91,
1724-1736.
|
|
|
|
|
|
|
Y.Lu,
Y.H.Zhang,
and
L.R.Lynd
(2006).
Enzyme-microbe synergy during cellulose hydrolysis by Clostridium thermocellum.
|
| |
Proc Natl Acad Sci U S A,
103,
16165-16169.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
|
 |
Links
