3GNF: P1 Crystal Structure Of The N-Terminal R1-R7 Of Murine Mvp

Citation:
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.
PDB ID: 3GNFDownload
MMDB ID: 77986
PDB Deposition Date: 2009/3/17
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 3GNF: monomeric; determined by author and by software (PISA)
Molecular Components in 3GNF
Label Count Molecule
Protein (1 molecule)
1
Major Vault Protein(Gene symbol: Mvp)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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