1CZ4

NMR STRUCTURE OF VAT-N: THE N-TERMINAL DOMAIN OF VAT (VCP-LIKE ATPASE OF THERMOPLASMA)

Summary for 1CZ4

• Entry DOI: 10.2210/pdb1cz4/pdb
• Related: 1CZ5
• Descriptor: VCP-LIKE ATPASE (1 entity in total)
• Functional Keywords: double-psi beta-barrel, beta-clam, substrate recognition domain, hydrolase
• Biological source: Thermoplasma acidophilum
• Total number of polymer chains: 1
• Total formula weight: 20649.82

Authors

Coles, M.,Diercks, T.,Liermann, J.,Groeger, A.,Rockel, B.,Baumeister, W.,Koretke, K.,Lupas, A.,Peters, J.,Kessler, H. (deposition date: 1999-09-01, release date: 1999-10-12, Last modification date: 2024-05-22)

Primary citation

Coles, M.,Diercks, T.,Liermann, J.,Groger, A.,Rockel, B.,Baumeister, W.,Koretke, K.K.,Lupas, A.,Peters, J.,Kessler, H.
The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple betaalphabetabeta element.
Curr.Biol., 9:1158-1168, 1999

PubMed Abstract: The VAT protein of the archaebacterium Thermoplasma acidophilum, like all other members of the Cdc48/p97 family of AAA ATPases, has two ATPase domains and a 185-residue amino-terminal substrate-recognition domain, VAT-N. VAT shows activity in protein folding and unfolding and thus shares the common function of these ATPases in disassembly and/or degradation of protein complexes.

PubMed: 10531028
DOI: 10.1016/S0960-9822(00)80017-2

Experimental method

SOLUTION NMR