1OVX
NMR structure of the E. coli ClpX chaperone zinc binding domain dimer
Summary for 1OVX
| Entry DOI | 10.2210/pdb1ovx/pdb |
| Descriptor | ATP-dependent Clp protease ATP-binding subunit clpX, ZINC ION (2 entities in total) |
| Functional Keywords | treble clef zinc finger, homodimer, metal binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 15634.47 |
| Authors | Donaldson, L.W.,Kwan, J.,Wojtyra, U.,Houry, W.A. (deposition date: 2003-03-27, release date: 2003-12-30, Last modification date: 2024-05-01) |
| Primary citation | Donaldson, L.W.,Wojtyra, U.,Houry, W.A. Solution structure of the dimeric zinc binding domain of the chaperone ClpX. J.Biol.Chem., 278:48991-48996, 2003 Cited by PubMed Abstract: ClpX (423 amino acids), a member of the Clp/Hsp100 family of molecular chaperones and the protease, ClpP, comprise a multimeric complex supporting targeted protein degradation in Escherichia coli. The ClpX sequence consists of an NH2-terminal zinc binding domain (ZBD) and a COOH-terminal ATPase domain. Earlier, we have demonstrated that the zinc binding domain forms a constitutive dimer that is essential for the degradation of some ClpX substrates such as gammaO and MuA but is not required for the degradation of other substrates such as green fluorescent protein-SsrA. In this report, we present the NMR solution structure of the zinc binding domain dimer. The monomer fold reveals that ZBD is a member of the treble clef zinc finger family, a motif known to facilitate protein-ligand, protein-DNA, and protein-protein interactions. However, the dimeric ZBD structure is not related to any protein structure in the Protein Data Bank. A trimer-of-dimers model of ZBD is presented, which might reflect the closed state of the ClpX hexamer. PubMed: 14525985DOI: 10.1074/jbc.M307826200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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