PDBsum entry 3a2s

Membrane protein

PDB id: 3a2s

Contents

Protein chain

341 a.a. *

Ligands

GLC-FRU

LDA

Waters ×168

* Residue conservation analysis

PDB id:

3a2s

Name:

Membrane protein

Title:

Crystal structure of outer membrane protein porb from neisseria meningitidis in complex with sucrose

Structure:

Outer membrane protein ii. Chain: x. Engineered: yes

Source:

Neisseria meningitidis. Organism_taxid: 487. Gene: porb. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.211 R-free: 0.256

Authors:

M.Tanabe,T.M.Iverson

Key ref:

M.Tanabe et al. (2010). Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proc Natl Acad Sci U S A, 107, 6811-6816. PubMed id: 20351243

Date:

04-Jun-09 Release date: 07-Apr-10

Protein chain

Q5RT80  (Q5RT80_NEIME) -  Outer membrane protein II (Fragment) from Neisseria meningitidis

Seq: 322 a.a.

Struc: 341 a.a.

Proc Natl Acad Sci U S A 107:6811-6816 (2010)

PubMed id: 20351243

Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB.

M.Tanabe, C.M.Nimigean, T.M.Iverson.

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.