1CZ5
NMR STRUCTURE OF VAT-N: THE N-TERMINAL DOMAIN OF VAT (VCP-LIKE ATPASE OF THERMOPLASMA)
Summary for 1CZ5
| Entry DOI | 10.2210/pdb1cz5/pdb |
| Related | 1CZ4 |
| Descriptor | VCP-LIKE ATPASE (1 entity in total) |
| Functional Keywords | double-psi beta-barrel, beta-clam, substrate recognition domain, fusion protein, 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 Cited by 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: 10531028DOI: 10.1016/S0960-9822(00)80017-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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