3GF5

Crystal structure of the P21 R1-R7 N-terminal domain of murine MVP

Summary for 3GF5

• Entry DOI: 10.2210/pdb3gf5/pdb
• Related: 3GNF 3GNG
• Descriptor: Major vault protein, GLYCEROL (3 entities in total)
• Functional Keywords: beta sheets, phosphoprotein, ribonucleoprotein, structural protein
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm: Q9EQK5
• Total number of polymer chains: 2
• Total formula weight: 88116.21

Authors

Querol-Audi, J.,Casanas, A.,Luque, D.,Caston, J.R.,Fita, I.,Verdaguer, N. (deposition date: 2009-02-26, release date: 2009-11-10, Last modification date: 2024-03-20)

Primary citation

Querol-Audi, J.,Casanas, A.,Uson, I.,Luque, D.,Caston, J.R.,Fita, I.,Verdaguer, N.
The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP
Embo J., 28:3450-3457, 2009

PubMed Abstract: 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 A resolution, together with the 2.1-A structure of the seven N-terminal domains (R1-R7) of MVP, reveal the interactions governing vault association and provide an explanation for a reversible dissociation induced by low pH. The structural comparison with the recently published 3.5 A model shows major discrepancies, both in the main chain tracing and in the side chain assignment of the two terminal domains R1 and R2.

PubMed: 19779459
DOI: 10.1038/emboj.2009.274

Experimental method

X-RAY DIFFRACTION (2.5 Å)