Item request has been placed!
×
Item request cannot be made.
×
Processing Request
Substrate-induced exposure of an energy-coupling motif of a membrane transporter.
Item request has been placed!
×
Item request cannot be made.
×
Processing Request
- المؤلفون: Merianos HJ;Merianos HJ; Cadieux N; Lin CH; Kadner RJ; Cafiso DS
- المصدر:
Nature structural biology [Nat Struct Biol] 2000 Mar; Vol. 7 (3), pp. 205-9.
- نوع النشر :
Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
- اللغة:
English
- معلومة اضافية
- المصدر:
Publisher: Nature Pub. Co Country of Publication: United States NLM ID: 9421566 Publication Model: Print Cited Medium: Print ISSN: 1072-8368 (Print) Linking ISSN: 10728368 NLM ISO Abbreviation: Nat Struct Biol Subsets: MEDLINE
- بيانات النشر:
Original Publication: New York, NY : Nature Pub. Co., c1994-c2003.
- الموضوع:
- نبذة مختصرة :
BtuB is an outer membrane protein responsible for the uptake of vitamin B12 by Escherichia coli. It belongs to a family of bacterial transport proteins that derive energy for transport by coupling to the trans-periplasmic energy-coupling protein TonB. Using site-directed spin labeling and EPR we investigated the structure and substrate-induced changes in the TonB box, a highly conserved region in all TonB dependent transporters that may couple to TonB. In the absence of substrate, the line widths and collision parameters from EPR are consistent with this domain existing in a structured helical conformation that contacts the barrel of the transporter. Addition of substrate converts this segment into an extended structure that is highly dynamic, disordered and probably extended into the periplasm. This structural change demonstrates that the TonB box cycles between sequestered and accessible states in a substrate-dependent fashion. In a transport defective mutant of BtuB, this conformational cycle is disrupted and the TonB box appears to be extended even in the absence of substrate. These data suggest that the TonB box extends into the periplasm and interacts with TonB only in
- Grant Information:
R01 GM035215 United States GM NIGMS NIH HHS
- الرقم المعرف:
0 (Bacterial Outer Membrane Proteins)
0 (Bacterial Proteins)
0 (BtuB protein, E coli)
0 (Escherichia coli Proteins)
0 (Membrane Proteins)
0 (Membrane Transport Proteins)
0 (Receptors, Peptide)
0 (Spin Labels)
0 (tonB protein, Bacteria)
0 (tonB protein, E coli)
P6YC3EG204 (Vitamin B 12)
- الموضوع:
Date Created: 20000304 Date Completed: 20000407 Latest Revision: 20170426
- الموضوع:
20221213
- الرقم المعرف:
10.1038/73309
- الرقم المعرف:
10700278
No Comments.