Out now as a preprint, “Molecular basis of mitochondrial leucine transport by human Sideroflexin 1”. #CryoEM #Mitochondria #StructuralBiology www.biorxiv.org/content/10.6...
Chancie T
@chanciet.bsky.social
Lead Scientist (Cryo-EM) @ Nxera Pharma 🇬🇧 Lab alumni: @cpaulino.bsky.social & @membraneenzymology.bsky.social (Slotboom) @ RUG 🇳🇱 & @mitocarriers.bsky.social (Kunji) @ MRC MBU/Cambridge University 🇬🇧 #MembraneProteins, #Transporters, #GPCRs, #cryoEM, #SBDD
Our new Review on the emerging structural context for UCP1 from brown adipose tissue onlinelibrary.wiley.com/doi/10.1111/...
A Structural Context for the Mechanisms of Uncoupling Protein 1 in Brown Fat Thermogenesis
Uncoupling Protein 1 (UCP1) is a defining feature of brown fat and facilitates the specialized ability of the tissue to generate heat in the process of non-shivering thermogenesis. The protein is act...
onlinelibrary.wiley.com
Our paper on the proton-driven secondary active #transporter SbmA for antimicrobial peptides is finally out! We used #cryoEM, #EPR, #MD to show that it resembles and undergoes conformational changes like #ABC transporter TMDs consistent with an alternating-access transport mechanism.
Shared structural mechanisms of alternating access between the secondary peptide transporter SbmA and ABC transporters - Nature Communications
SbmA is a proton-driven transporter that imports antimicrobial peptides andstructurally resembles the transmembrane domain of ABC-transporters. Here, authors show through cryo-EM structures, EPR spect...
doi.org
Chancie T@chanciet.bsky.social · 2y agoCheck out our new preprint on the bacterial secondary active #transporter SbmA.
Here, we critically review the structures of the mitochondrial pyruvate carrier (MPC) in apo and ligand-bound states, highlighting controversies with regard to the orientation in the inner membrane, interpretation of the transport states, and modelling of the inhibitors. doi.org/10.1016/j.ti...
Redirecting
doi.org
Our review on the peculiar properties of mitochondrial carriers of the SLC25 family out: portlandpress.com/biochemj/art...
Solène’s 4.5 years of postdoctoral work in our lab (she started just before the corona pandemic) has now been published. A heroic effort that revealed -at the single molecule level- that ATP drives the dissociation of an ECF transporter complex under turnover conditions. See rdcu.be/elTKc
Single-molecule visualization of ATP-induced dynamics of the subunit composition of an ECF transporter complex under turnover conditions
Nature Communications - The association and dissociation dynamics of the ECF transporter complex for vitamin B12 are visualized by single-molecule FRET, highlighting the original transport...
rdcu.be
A colder frontier in cryo-EM 🧪🔬 Chris Russo’s group, inc. Joshua Dickerson, adapted #cryoEM to work at liquid helium temperatures (13 kelvins), where every frame captured contains more information than the equivalent using liquid nitrogen (81 kelvins). Read more: tinyurl.com/mwwcunkc #LMBResearch
Our paper is finally out: Molecular basis of pyruvate transport and inhibition of the human mitochondrial pyruvate carrier | Science Advances www.science.org/doi/10.1126/... #mitochondria #cryo-EM
Molecular basis of pyruvate transport and inhibition of the human mitochondrial pyruvate carrier
The mitochondrial pyruvate carrier transport mechanism is ΔpH driven and is inhibited competitively by distinct compound classes.
science.org
Check out our new preprint on the bacterial secondary active #transporter SbmA.
Shared structural mechanisms of alternating access between the secondary peptide transporter SbmA and ABC transporters
SbmA is a membrane transporter from Escherichia coli that imports antimicrobial peptides. Although the protein is a secondary transporter that is energized by the proton gradient, it is structurally r...
dx.doi.org
The work was a collaboration with Nate Traaseth. Hope the method will help others solve structures of small membrane proteins in multiple conformations. The fusion strategy can be seen as a tribute to the late Ron Kaback, who attempted a similar approach with crystallizing the LacY 30 years ago.
David B. Sauer@davidbsauer.bsky.social · 2y agoA standardized method for determining MFS structures! Fantastic work by the Traaseth and @danengw.bsky.social labs Looking forward to bringing this platform in-house! doi.org/10.1038/s414...
At the heart of biology is the mantra: structure dictates function.Biological structures are also beautiful in their intricacy. David Goodsell brought this into public view. As he leaves "Molecule of the Month". here's a huge thank you for helping me see more clearly🧪1/2 cdn.rcsb.org/rcsb-pdb/gen...
Using 33 pathogenic variants of citrin we identify crucial elements of the carrier domain required for transport and show that the N-terminal domain is not involved in calcium regulation of transport, but causes a mitochondrial import defect, when mutated. www.sciencedirect.com/science/arti...
Distinct roles for the domains of the mitochondrial aspartate/glutamate carrier citrin in organellar localization and substrate transport
Citrin, the mitochondrial aspartate/glutamate carrier isoform 2 (AGC2), is structurally and mechanistically the most complex SLC25 family member, beca…
sciencedirect.com
Our new paper is out! #mitochondria #transporters #adeninetranslocase #SLC25 www.science.org/doi/10.1126/...
Membrane potential stimulates ADP import and ATP export by the mitochondrial ADP/ATP carrier due to its positively charged binding site
Reorientation of a positively charged binding site drives adenine nucleotide exchange in the presence of a membrane potential.
science.org