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3A2S

Crystal Structure of outer membrane protein PorB from Neisseria meningitidis in complex with sucrose

Summary for 3A2S
Entry DOI10.2210/pdb3a2s/pdb
Related3A2R 3A2T 3A2U
Related PRD IDPRD_900003
DescriptorOuter membrane protein II, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, LAURYL DIMETHYLAMINE-N-OXIDE, ... (4 entities in total)
Functional Keywordsbeta barrel, outer membrane protein, porin, neisseria meningitidis, cell membrane, cell outer membrane, ion transport, membrane, transmembrane, transport protein, immune system, membrane protein
Biological sourceNeisseria meningitidis
Total number of polymer chains1
Total formula weight38751.00
Authors
Tanabe, M.,Iverson, T.M. (deposition date: 2009-06-04, release date: 2010-04-07, Last modification date: 2023-11-01)
Primary citationTanabe, M.,Nimigean, C.M.,Iverson, T.M.
Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB.
Proc.Natl.Acad.Sci.USA, 107:6811-6816, 2010
Cited by
PubMed Abstract: 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.
PubMed: 20351243
DOI: 10.1073/pnas.0912115107
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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