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PDBsum entry 4jrf
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Cell adhesion
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PDB id
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4jrf
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References listed in PDB file
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Key reference
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Title
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A distinct type of pilus from the human microbiome.
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Authors
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Q.Xu,
M.Shoji,
S.Shibata,
M.Naito,
K.Sato,
M.A.Elsliger,
J.C.Grant,
H.L.Axelrod,
H.J.Chiu,
C.L.Farr,
L.Jaroszewski,
M.W.Knuth,
A.M.Deacon,
A.Godzik,
S.A.Lesley,
M.A.Curtis,
K.Nakayama,
I.A.Wilson.
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Ref.
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Cell, 2016,
165,
690-703.
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PubMed id
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Abstract
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Pili are proteinaceous polymers of linked pilins that protrude from the cell
surface of many bacteria and often mediate adherence and virulence. We
investigated a set of 20 Bacteroidia pilins from the human microbiome whose
structures and mechanism of assembly were unknown. Crystal structures and
biochemical data revealed a diverse protein superfamily with a common Greek-key
β sandwich fold with two transthyretin-like repeats that polymerize into a
pilus through a strand-exchange mechanism. The assembly mechanism of the
central, structural pilins involves proteinase-assisted removal of their
N-terminal β strand, creating an extended hydrophobic groove that binds the
C-terminal donor strands of the incoming pilin. Accessory pilins at the tip and
base have unique structural features specific to their location, allowing
initiation or termination of the assembly. The Bacteroidia pilus, therefore, has
a biogenesis mechanism that is distinct from other known pili and likely
represents a different type of bacterial pilus.
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