 |
PDBsum entry 3iyh
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
* C-alpha coords only
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Virus
|
|
|
Title:
|
|
P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical cross-links
|
|
Structure:
|
|
Coat protein. Chain: a, b, c, d, e, f. Synonym: protein gp5
|
|
Source:
|
|
Enterobacteria phage p22. Bacteriophage p22. Organism_taxid: 10754
|
|
Authors:
|
|
K.N.Parent,R.Khayat,L.H.Tu,M.M.Suhanovsky,J.R.Cortines,C.M.Teschke, J.E.Johnson,T.S.Baker
|
|
Key ref:
|
|
K.N.Parent
et al.
(2010).
P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks.
Structure,
18,
390-401.
PubMed id:
|
|
|
Date:
|
|
|
14-Dec-09
|
Release date:
|
31-Mar-10
|
|
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P26747
(CAPSD_BPP22) -
Major capsid protein from Salmonella phage P22
|
|
|
|
Seq:
Struc:
|
|
|
|
430 a.a.
391 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Structure
18:390-401
(2010)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks.
|
|
K.N.Parent,
R.Khayat,
L.H.Tu,
M.M.Suhanovsky,
J.R.Cortines,
C.M.Teschke,
J.E.Johnson,
T.S.Baker.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Viral capsid assembly and stability in tailed, dsDNA phage and Herpesviridae are
achieved by various means including chemical crosslinks (unique to HK97), or
auxiliary proteins (lambda, T4, phi29, and herpesviruses). All these viruses
have coat proteins (CP) with a conserved, HK97-like core structure. We used a
combination of trypsin digestion, gold labeling, cryo-electron microscopy, 3D
image reconstruction, and comparative modeling to derive two independent,
pseudoatomic models of bacteriophage P22 CP: before and after maturation. P22
capsid stabilization results from intersubunit interactions among N-terminal
helices and an extensive "P loop," which obviate the need for crosslinks or
auxiliary proteins. P22 CP also has a telokin-like Ig domain that likely
stabilizes the monomer fold so that assembly may proceed via individual subunit
addition rather than via preformed capsomers as occurs in HK97. Hence, the P22
CP structure may be a paradigm for understanding how monomers assemble in
viruses like phi29 and HSV-1.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
D.H.Chen,
M.L.Baker,
C.F.Hryc,
F.DiMaio,
J.Jakana,
W.Wu,
M.Dougherty,
C.Haase-Pettingell,
M.F.Schmid,
W.Jiang,
D.Baker,
J.A.King,
and
W.Chiu
(2011).
Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus.
|
| |
Proc Natl Acad Sci U S A,
108,
1355-1360.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
K.N.Parent,
R.S.Sinkovits,
M.M.Suhanovsky,
C.M.Teschke,
E.H.Egelman,
and
T.S.Baker
(2010).
Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins.
|
| |
Phys Biol,
7,
045004.
|
|
|
|
|
|
|
M.M.Suhanovsky,
K.N.Parent,
S.E.Dunn,
T.S.Baker,
and
C.M.Teschke
(2010).
Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.
|
| |
Mol Microbiol,
77,
1568-1582.
|
|
|
|
|
|
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
codes are
shown on the right.
|
|
Links
