2DS5

Structure of the ZBD in the orthorhomibic crystal from

Summary for 2DS5

• Entry DOI: 10.2210/pdb2ds5/pdb
• Related: 2DS6 2DS7 2DS8
• Descriptor: ATP-dependent Clp protease ATP-binding subunit clpX, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: treble cleft zinc finger, metal binding protein, protein binding
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 11882.38

Authors

Song, H.K.,Park, E.Y.,Lee, B.G.,Hong, S.B. (deposition date: 2006-06-22, release date: 2007-02-13, Last modification date: 2023-10-25)

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

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: 17258768
DOI: 10.1016/j.jmb.2007.01.003

Experimental method

X-RAY DIFFRACTION (1.5 Å)