1Y7X

Solution structure of a two-repeat fragment of major vault protein

Summary for 1Y7X

• Entry DOI: 10.2210/pdb1y7x/pdb
• NMR Information: BMRB: 6447
• Descriptor: Major vault protein (1 entity in total)
• Functional Keywords: structural repeats, beta-sheet modules, structural protein, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q14764
• Total number of polymer chains: 1
• Total formula weight: 12772.56

Authors

Kozlov, G.,Vavelyuk, O.,Minailiuc, O.,Banville, D.,Gehring, K.,Ekiel, I. (deposition date: 2004-12-10, release date: 2005-12-20, Last modification date: 2024-05-22)

Primary citation

Kozlov, G.,Vavelyuk, O.,Minailiuc, O.,Banville, D.,Gehring, K.,Ekiel, I.
Solution structure of a two-repeat fragment of major vault protein.
J.Mol.Biol., 356:444-452, 2006

PubMed Abstract: Major vault protein (MVP) is the main constituent of vaults, large ribonucleoprotein particles implicated in resistance to cancer therapy and correlated with poor survival prognosis. Here, we report the structure of the main repeat element in human MVP. The approximately 55 amino acid residue MVP domain has a unique, novel fold that consists of a three-stranded antiparallel beta-sheet. The solution NMR structure of a two-domain fragment reveals the interdomain contacts and relative orientations of the two MVP domains. We use these results to model the assembly of 672 MVP domains from 96 MVP molecules into the ribs of the 13MDa vault structure. The unique features include a thin, skin-like structure with polar residues on both the cytoplasmic and internal surface, and a pole-to-pole arrangement of MVP molecules. These studies provide a starting point for understanding the self-assembly of MVP into vaults and their interactions with other proteins. Chemical shift perturbation studies identified the binding site of vault poly(ADP-ribose) polymerase, another component of vault particles, indicating that MVP domains form a new class of interaction-mediating modules.

PubMed: 16373071
DOI: 10.1016/j.jmb.2005.11.064

Experimental method

SOLUTION NMR