3A2S
Crystal Structure of outer membrane protein PorB from Neisseria meningitidis in complex with sucrose
Summary for 3A2S
| Entry DOI | 10.2210/pdb3a2s/pdb |
| Related | 3A2R 3A2T 3A2U |
| Related PRD ID | PRD_900003 |
| Descriptor | Outer membrane protein II, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, LAURYL DIMETHYLAMINE-N-OXIDE, ... (4 entities in total) |
| Functional Keywords | beta barrel, outer membrane protein, porin, neisseria meningitidis, cell membrane, cell outer membrane, ion transport, membrane, transmembrane, transport protein, immune system, membrane protein |
| Biological source | Neisseria meningitidis |
| Total number of polymer chains | 1 |
| Total formula weight | 38751.00 |
| Authors | Tanabe, M.,Iverson, T.M. (deposition date: 2009-06-04, release date: 2010-04-07, Last modification date: 2023-11-01) |
| 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 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: 20351243DOI: 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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