Surface loop motion in FepA
Open accessAbstract
Using a lysine-specific cleavable cross-linking reagent ethylene glycolbis(sulfosuccimidylsuccinate) (Sulfo-EGS), we studied conformational motion in the surface loops of Escherichia coli FepA during its transport of the siderophore ferric enterobactin. Site-directed mutagenesis determined that Sulfo-EGS reacted with two lysines, K332 and K483, and at least two other unidentified Lys residues in the surface loops of the outer membrane protein. The reagent cross-linked K483 in FepA L7 to either K332 in L5, forming a product that we designated band 1, or to the major outer membrane proteins OmpF, OmpC, and OmpA, forming band 2. Ferric enterobactin binding to FepA did not prevent modification of K483 by Sulfo-EGS but blocked its cross-linking to OmpF/C and OmpA and reduced its coupling to K332. These data show that the loops of FepA undergo conformational changes in vivo, with an approximate magnitude of 15 A, from a ligand-free open state to a ligand-bound closed state. The coupling of FepA L7 to OmpF, OmpC, or OmpA was TonB independent and was unaffected by the uncouplers CCCP (carbonyl cyanide m-chlorophenylhydrazone) and DNP (2,4-dinitrophenol) but completely inhibited by cyanide.
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Fiu mimics the induced fit binding mechanisms of FepA and FecA as they close around their iron complexes.
“However, in this respect, Fiu mimics the induced fit binding mechanisms of FepA ( Scott et al., 2002 ; Smallwood et al., 2014 ) and FecA ( Ferguson et al., 2002 ) as they close around their iron complexes.”
From Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu (2024) · cites this paper as Scott et al., 2002
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- [38]Scott, D. C. 2001. Ph.D. dissertation. University of Oklahoma, Norman.
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- Authors
- Scott, D. C., Newton, S. M. C., & Klebba, P. E.
- Affiliations
- University of Oklahoma (US)
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2002-09
- Volume
- 184
- Issue
- 17
- Pages
- 4906-4911
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC135268
- OpenAlex
- W2168417777
- Cited by
- 35
- References
- 47
- Citations by year
- 2024: 1 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 1 · 2017: 1 · 2016: 1 · 2014: 2 · 2013: 2 · 2012: 1
- FWCI
- 1.77
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Oklahoma Center for the Advancement of Science and Technology
- National Institutes of Health
- National Institute of General Medical Sciences (GM 53836, R01GM053836)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- FepA, siderophore transport, outer membrane proteins, lysine cross-linking, OmpF, OmpC, OmpA, TonB, Escherichia coli
- MeSH terms
- Bacterial Outer Membrane Proteins, Carrier Proteins, Ligands, Protein Conformation, Receptors, Cell Surface, Porins
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