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PDBsum entry 3iyh
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References listed in PDB file
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Key reference
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Title
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P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks.
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Authors
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K.N.Parent,
R.Khayat,
L.H.Tu,
M.M.Suhanovsky,
J.R.Cortines,
C.M.Teschke,
J.E.Johnson,
T.S.Baker.
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Ref.
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Structure, 2010,
18,
390-401.
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PubMed id
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Abstract
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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.
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Headers
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