2DS7
Structure of the ZBD in the hexagonal crystal form
Summary for 2DS7
| Entry DOI | 10.2210/pdb2ds7/pdb |
| Related | 2DS5 2DS6 2DS8 |
| Descriptor | ATP-dependent Clp protease ATP-binding subunit clpX, ZINC ION (3 entities in total) |
| Functional Keywords | c43m mutant, zinc binding domain of clpx, selenomethionine incorporation, metal binding protein, protein binding |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 5898.99 |
| Authors | Park, E.Y.,Lee, B.G.,Hong, S.B.,Song, H.K. (deposition date: 2006-06-22, release date: 2007-02-13, Last modification date: 2024-10-16) |
| Primary citation | Park, E.Y.,Lee, B.G.,Hong, S.B.,Kim, H.W.,Jeon, H.,Song, H.K. Structural Basis of SspB-tail Recognition by the Zinc Binding Domain of ClpX. J.Mol.Biol., 367:514-526, 2007 Cited by PubMed Abstract: The degradation of ssrA(AANDENYALAA)-tagged proteins in the bacterial cytosol is carried out by the ClpXP protease and is markedly stimulated by the SspB adaptor protein. It has previously been reported that the amino-terminal zinc-binding domain of ClpX (ZBD) is involved in complex formation with the SspB-tail (XB: ClpX-binding motif). In an effort to better understand the recognition of SspB by ClpX and the mechanism of delivery of ssrA-tagged substrates to ClpXP, we have determined the structures of ZBD alone at 1.5, 2.0, and 2.5 A resolution in each different crystal form and also in complex with XB peptide at 1.6 A resolution. The XB peptide forms an antiparallel beta-sheet with two beta-strands of ZBD, and the structure shows a 1:1 stoichiometric complex between ZBD and XB, suggesting that there are two independent SspB-tail-binding sites in ZBD. The high-resolution ZBD:XB complex structure, in combination with biochemical analyses, can account for key determinants in the recognition of the SspB-tail by ClpX and sheds light on the mechanism of delivery of target proteins to the prokaryotic degradation machine. PubMed: 17258768DOI: 10.1016/j.jmb.2007.01.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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