3VZT

Crystal Structure of outer membrane protein PorB from Neisseria meningitidis

Replaces:  3A2R

Summary for 3VZT

• Entry DOI: 10.2210/pdb3vzt/pdb
• Related: 3VZU 3VZW
• Descriptor: outer membrane protein, CESIUM ION (3 entities in total)
• Functional Keywords: beta-barrel, porin, channel, outer membrane protein, transport, membrane protein
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 1
• Total formula weight: 38578.02

Authors

Tanabe, M.,Iverson, T.M. (deposition date: 2012-10-15, release date: 2012-11-07, Last modification date: 2024-03-20)

Primary citation

Tanabe, 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

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)