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PDBsum entry 3a2s
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Membrane protein
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PDB id
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3a2s
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References listed in PDB file
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Key reference
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Title
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Structural basis for solute transport, Nucleotide regulation, And immunological recognition of neisseria meningitidis porb.
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Authors
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M.Tanabe,
C.M.Nimigean,
T.M.Iverson.
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Ref.
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Proc Natl Acad Sci U S A, 2010,
107,
6811-6816.
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PubMed id
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Abstract
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PorB is the second most prevalent outer membrane protein in Neisseria
meningitidis. PorB is required for neisserial pathogenesis and can elicit a
Toll-like receptor mediated host immune response. Here, the x-ray crystal
structure of PorB has been determined to 2.3 A resolution. Structural analysis
and cocrystallization studies identify three putative solute translocation
pathways through the channel pore: One pathway transports anions nonselectively,
one transports cations nonselectively, and one facilitates the specific uptake
of sugars. During infection, PorB likely binds host mitochondrial ATP, and
cocrystallization with the ATP analog AMP-PNP suggests that binding of
nucleotides regulates these translocation pathways both by partial occlusion of
the pore and by restricting the motion of a putative voltage gating loop. PorB
is located on the surface of N. meningitidis and can be recognized by receptors
of the host innate immune system. Features of PorB suggest that Toll-like
receptor mediated recognition outer membrane proteins may be initiated with a
nonspecific electrostatic attraction.
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