Structural Biology
- Structural roles of Ump1 and β-subunit propeptides in proteasome biogenesis
A 2.1 Å cryo-EM structure of a late proteasome precursor reveals roles of the assembly chaperone Ump1 and β-subunit propeptides in proteasome biogenesis.
- Cryo-EM reveals a phosphorylated R-domain envelops the NBD1 catalytic domain in an ABC transporter
Cryo-EM reveals that the R-domain of an ABCC transporter encircles the ATP catalytic domain-1 in a tetra-phosphorylated manner and regulates the ATPase activity along with cellular transport.
- Activation mechanism and novel binding sites of the BKCa channel activator CTIBD
CTIBD relieves overactive bladder in animal models by activating BKCa channels through extracellular binding, independent of calcium and membrane depolarization; key residues include W22, W203, and F266.
- pyRBDome: a comprehensive computational platform for enhancing RNA-binding proteome data
This study explores enhancing protein–RNA interaction prediction using machine learning.
- Structure of the human systemic RNAi defective transmembrane protein 1 (hSIDT1) reveals the conformational flexibility of its lipid binding domain
This study reports a cryo-EM structure of a small non-coding RNA transporter, hSIDT1, and delineates the role of lipid in the conformational dynamics of the lipid binding domain of hSIDT1.
- Exploring the molecular composition of the multipass translocon in its native membrane environment
Cryo-ET reveals the compositional variability of the multipass translocon complex dependent on translational activity of the bound ribosome and suggests the location of its subunit NOMO.
- PrgE: an OB-fold protein from plasmid pCF10 with striking differences to prototypical bacterial SSBs
Enterococcal PrgE, from the conjugative plasmid pCF10, is a non-typical SSB that not only binds ssDNA in a filamentous manner but also binds dsDNA equally well as ssDNA.
- Molecular mechanism for recognition of the cargo adapter Rab6GTP by the dynein adapter BicD2
We present a structural model for recognition of a key modulator of protein secretion, Rab6GTP, by the dynein adapter BicD2, which provides new insights into the trafficking of secretory vesicles.
- Subdomains of the Helicobacter pylori Cag T4SS outer membrane core complex exhibit structural independence
Structural and proteomic analyses of H. pylori Cag T4SSs purified from deletion mutants highlight the unexpected structural independence between the OMC and PR, two major subdomains of this complex.
- Structural basis of translation inhibition by a valine tRNA-derived fragment
We analyzed three structures of Val-tRF-30S ribosomal complexes, which revealed the mechanism by which val-tRF inhibits protein translation. The mechanism includes the binding of val-tRNA to the decoding site, inhibiting the binding of tRNA-mRNA, and inhibiting the binding of aIF1A.