The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP
@article{QuerolAudi2009TheMO, title={The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP}, author={Jordi Querol-Audí and Arnau Casa{\~n}as and Isabel Us{\'o}n and Daniel Luque and Jos{\'e} R. Cast{\'o}n and Ignasi Fita and N{\'u}ria Verdaguer}, journal={The EMBO Journal}, year={2009}, volume={28}, pages={3450 - 3457} }
Vaults are ubiquitous ribonucleoprotein complexes involved in a diversity of cellular processes, including multidrug resistance, transport mechanisms and signal transmission. The vault particle shows a barrel‐shaped structure organized in two identical moieties, each consisting of 39 copies of the major vault protein MVP. Earlier data indicated that vault halves can dissociate at acidic pH. The crystal structure of the vault particle solved at 8 Å resolution, together with the 2.1‐Å structure…
32 Citations
Structural Dynamics of the Vault Ribonucleoprotein Particle
- Biology
- 2012
The high resolution, crystal structure of the of the seven N-terminal domains of MVP, forming the central vault barrel, revealed the interactions governing vault association and suggested a pH-dependent mechanism for a reversible dissociation induced by low pH.
Structural studies of large nucleoprotein particles, vaults
- BiologyProceedings of the Japan Academy. Series B, Physical and biological sciences
- 2012
Vault is the largest nonicosahedral cytosolic nucleoprotein particle ever described. The widespread presence and evolutionary conservation of vaults suggest important biologic roles, although their…
Symmetry disruption commits vault particles to disassembly
- BiologyScience advances
- 2022
The molecular determinants for the vault opening process are characterized using a combination of vault recombinant reconstitution and structural techniques to inform a hitherto uncharacterized step of the vault cycle and will aid current engineering efforts leveraging vault for tailored cargo delivery.
Solution Structures of Engineered Vault Particles
- ChemistryStructure
- 2018
Vaults obtained by engineering at the N terminus of rat major vault protein an HIV-1 Gag protein segment are determined and their near-atomic resolution structures are determined in a solution/non-crystalline environment.
Bacterial Major Vault Protein homologs shed new light on origins of the enigmatic organelle
- BiologybioRxiv
- 2019
It is speculated that the most likely scenario for vault appearance in eukaryotes is horizontal gene transfer from cyanobacteria, and it was shown that MVP sequences from chemotrophic bacteria Myxococcales and Cytophagales contain a domain homologous to Eukaryotic band-7 domain, unlike cyanobacterial and eukARYotic major vault proteins.
The Vault Nanoparticle: A Gigantic Ribonucleoprotein Assembly Involved in Diverse Physiological and Pathological Phenomena and an Ideal Nanovector for Drug Delivery and Therapy
- BiologyCancers
- 2021
A better understanding of the physiological roles of this ribonucleoproteic complex may help develop new therapeutic strategies capable of coping with cancer progression and extend the scope of its exploitation as a nanocarrier for drug delivery.
New features of vault architecture and dynamics revealed by novel refinement using the deformable elastic network approach.
- ChemistryActa crystallographica. Section D, Biological crystallography
- 2013
Re-refinement of the vault structure by incorporating the high-resolution information available for the R1-7 domains, using the deformable elastic network (DEN) approach and maintaining strict 39-fold noncrystallographic symmetry is reported.
Direct visualization of vaults within intact cells by electron cryo-tomography
- BiologyCellular and Molecular Life Sciences
- 2015
These studies confirm that intracellular vaults are similar in overall size and shape to purified and recombinant vaults previously analyzed, and observe that vaults located in the extreme periphery of the cytoplasm predominately associate with granule-like structures and actin.
Structure of internalin InlK from the human pathogen Listeria monocytogenes.
- BiologyJournal of molecular biology
- 2013
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