ArticleBiophysical journal2006
Solutes modify a conformational transition in a membrane transport protein.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- Extracellular loops of BtuB facilitate transport of vitamin B12 through the outer membrane of E. coli.PLoS computational biology · 2020Article
- Simple Selection Procedure to Distinguish between Static and Flexible Loops.International journal of molecular sciences · 2020Article
- Effect of osmolytes on the binding of EGR1 transcription factor to DNA.Biopolymers · 2015Article
- Spin labeling and Double Electron-Electron Resonance (DEER) to Deconstruct Conformational Ensembles of HIV Protease.Methods in enzymology · 2015Article
- Identifying and quantitating conformational exchange in membrane proteins using site-directed spin labeling.Accounts of chemical research · 2014Review
- The juxtamembrane linker of full-length synaptotagmin 1 controls oligomerization and calcium-dependent membrane binding.The Journal of biological chemistry · 2014Article
- Pulsed EPR distance measurements in soluble proteins by site-directed spin labeling (SDSL).Current protocols in protein science · 2013Article
- Probing Protein Secondary Structure using EPR: Investigating a Dynamic Region of Visual Arrestin.Applied magnetic resonance · 2012Article
- Inter-spin distance determination using L-band (1-2 GHz) non-adiabatic rapid sweep electron paramagnetic resonance (NARS EPR).Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- Induced conformational changes in the activation of the Pseudomonas aeruginosa type III toxin, ExoU.Biophysical journal · 2011Article
- Conformational exchange in a membrane transport protein is altered in protein crystals.Biophysical journal · 2010Article
- Osmolytes modulate conformational exchange in solvent-exposed regions of membrane proteins.Protein science : a publication of the Protein Society · 2010Article
- Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins.Protein science : a publication of the Protein Society · 2009Article
- Gating at both ends and breathing in the middle: conformational dynamics of TolC.Biophysical journal · 2008Article
- Osmotically induced helix-coil transition in poly(glutamic acid).Biophysical journal · 2008Article
- Sequence of late molecular events in the activation of rhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Substrate-dependent transmembrane signaling in TonB-dependent transporters is not conserved.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Membrane simulations of OpcA: gating in the loops?Biophysical journal · 2007Article
- Structural and dynamical changes in an alpha-subunit of a heterotrimeric G protein along the activation pathway.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance.Biochemistry · 2006Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The bacterial outer-membrane vitamin B(12) transporter, BtuB, undergoes a dramatic order-to-disorder transition in its N-terminal energy-coupling motif (Ton box) upon substrate binding. Here, site-directed spin labeling (SDSL) is used to show that a range of solutes prevents this conformational change when ligand is bound to BtuB, resulting in a more ordered Ton box structure. For each solute examined, the data indicate that solutes effectively block this conformational transition through an osmotic mechanism. The molecular weight dependence of this solute effect has been examined for a series of polyethylene glycols, and a sharp molecular weight cutoff is observed. This cutoff indicates that solutes are preferentially excluded from a cavity within the protein as well as the protein surface. Furthermore, the sensitivity of the conformational change to solution osmolality is consistent with a structural model predicted by SDSL. When the Ton box is unfolded by detergents or mutations (rather than by ligand binding), solutes, such as polyethylene glycols and salts, also induce a more structured compacted conformation. These results suggest that conformational changes in this class of outer membrane transporters, which involve modest energy differences and changes in hydration, may be modulated by a range of solutes, including solutes typically used in protein crystallization.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.