Substrate-Induced Conformational Changes of the Perplasmic N-Terminus of an Outer-Membrane Transporter by Site-Directed Spin Labeling†

Biochemistry ◽  
2003 ◽  
Vol 42 (6) ◽  
pp. 1391-1400 ◽  
Author(s):  
Gail E. Fanucci ◽  
Kelly A. Coggshall ◽  
Nathalie Cadieux ◽  
Miyeon Kim ◽  
Robert J. Kadner ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Conformational Changes ◽  
Spin Labeling ◽  
Membrane Transporter ◽  
N Terminus ◽  
Outer Membrane Transporter ◽  
Site Directed Spin Labeling

scholarly journals Disulfide Chaperone Knockouts Enable In Vivo Double Spin Labeling of an Outer Membrane Transporter

2019 ◽  
Vol 117 (8) ◽  
pp. 1476-1484 ◽  
Author(s):  
Thushani D. Nilaweera ◽  
David A. Nyenhuis ◽  
Robert K. Nakamoto ◽  
David S. Cafiso
Keyword(s):  
Outer Membrane ◽  
Spin Labeling ◽  
Membrane Transporter ◽  
Double Spin ◽  
Outer Membrane Transporter

scholarly journals Identification and characterization of Pseudomonas membrane transporters necessary for utilization of the siderophore pyridine-2,6-bis(thiocarboxylic acid) (PDTC)

Microbiology ◽  
2006 ◽  
Vol 152 (10) ◽  
pp. 3157-3166 ◽  
Author(s):  
Lynne H. Leach ◽  
Thomas A. Lewis
Keyword(s):  
Outer Membrane ◽  
Transcriptional Activation ◽  
Iron Acquisition ◽  
Membrane Transporters ◽  
Membrane Transporter ◽  
Inner Membrane ◽  
Thiocarboxylic Acid ◽  
Outer Membrane Transporter ◽  
Identification And Characterization

The compound pyridine-2,6-bis(thiocarboxylic acid) (PDTC) is known to be produced and excreted by three strains of Pseudomonas. Its reactivity includes the complete dechlorination of the environmental contaminant carbon tetrachloride. PDTC functions as a siderophore; however, roles as a ferric reductant and antimicrobial agent have also been proposed. PDTC function and regulation were further explored by characterizing the phenotypes of mutants in predicted membrane transporter genes. The functions of a predicted outer-membrane transporter (PdtK) and a predicted inner-membrane permease (PdtE) were examined in Pseudomonas putida DSM 3601. Uptake of iron from 55Fe(III):PDTC, and bioutilization of PDTC in a chelated medium, were dependent upon PdtK and PdtE. Another strain of P. putida (KT2440), which lacks pdt orthologues, showed growth inhibition by PDTC that could be relieved by introducing a plasmid containing pdtKCPE. Transcriptional activation in response to exogenously added PDTC (25 μM) was unaltered by the pdtK or pdtE mutations; each mutant showed activation of a pdt transcriptional reporter, indistinguishable from an isogenic PDTC utilization-proficient strain. The data demonstrate that PdtK and PdtE constitute a bipartite outer-membrane/inner-membrane transport system for iron acquisition from Fe(III):PDTC. Disruptions in this portion of the P. putida DSM 3601 pdt gene cluster do not abolish PDTC-dependent transcriptional signalling.

scholarly journals Coupling of Ca2+ and Substrate Binding in the Outer Membrane Transporter BtuB

2009 ◽  
Vol 96 (3) ◽  
pp. 272a
Author(s):  
James C. Gumbart ◽  
Michael C. Wiener ◽  
Emad Tajkhorshid
Keyword(s):  
Outer Membrane ◽  
Substrate Binding ◽  
Membrane Transporter ◽  
Outer Membrane Transporter
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