FepA with globular domain deletions lacks activity

Journal of Bacteriology

Volumn 184, Issue 19, 2002, Pages 5508-5512

  Vakharia, Hema L ^a   Postle, Kathleen ^a  

^a WASHINGTON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CARRIER PROTEIN; COLICIN B; COLICIN D; ENTEROCHELIN; GENE PRODUCT; OUTER MEMBRANE PROTEIN; PROTEIN FEPA; PROTEIN TONB; UNCLASSIFIED DRUG;

ARTICLE; CROSS LINKING; GENE CONSTRUCT; GENE DELETION; GENE EXPRESSION; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; STRAIN DIFFERENCE;

BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL PROTEINS; CARRIER PROTEINS; COLICINS; ENTEROBACTIN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE DELETION; MEMBRANE PROTEINS; RECEPTORS, CELL SURFACE;

NEGIBACTERIA;

EID: 0036778139     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.19.5508-5512.2002     Document Type: Article

References (30)

1. Molecular analysis of the Escherichia coli ferric enterobactin receptor FepA
2. Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport
3. Genetic suppression demonstrates direct interaction of TonB protein with outer membrane transport proteins in Escherichia coli
4. Stability studies of FhuA, a two-domain outer membrane protein from Escherichia coli
5. The β-barrel domain of FhuAA5-160 is sufficient for TonB-dependent FhuA activities of Escherichia coli
6. Bacterial solutions to the iron-supply problem
7. Crystal structure of the outer membrane active transporter FepA from Escherichia coli
8. Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter
9. Structural basis of gating by the outer membrane transporter FecA
10. Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
11. ExbB and ExbD do not function independently in TonB-dependent energy transduction
12. Suppression of the btuB451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB-dependent receptor proteins in the outer membrane of Escherichia coli
13. Quantitation of known components of the Escherichia coli TonB-dependent energy transduction system: TonB, ExbB, ExbD, and FepA
14. TonB interacts with nonreceptor proteins in the outer membrane of Escherichia coli
15. Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers
16. Ferric enterobactin transport system in Escherichia coli K12. Extraction, assay, and specificity of the outer membrane receptor
17. FhuA barrelcork hybrids are active transporters and receptors
18. Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions
19. Identification of TonB homologs in the family Enterobacteriaceae and evidence for conservation of TonB-dependent energy transduction complexes
20. Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB
21. Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
22. Import-defective colicin B derivatives mutated in the TonB box
23. Substrate-induced exposure of an energy-coupling motif of a membrane transporter
24. Ligand-induced conformational change in the ferrichromeiron receptor of Escherichia coli K12
25. Domains of colicin-M involved in uptake and activity
26. Active transport by customized beta-barrels
27. Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane
28. Exchangeability of N termini in the ligand-gated porins of Escherichia coli
29. Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA
30. The plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, binds its siderophore in the absence of the transmembrane barrel domain