2ds5
From Proteopedia
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Structure of the ZBD in the orthorhomibic crystal from
Overview
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.
About this Structure
2DS5 is a Single protein structure of sequence from Escherichia coli with ZN, CA and PG4 as ligands. Full crystallographic information is available from OCA.
Reference
Structural Basis of SspB-tail Recognition by the Zinc Binding Domain of ClpX., Park EY, Lee BG, Hong SB, Kim HW, Jeon H, Song HK, J Mol Biol. 2007 Mar 23;367(2):514-26. Epub 2007 Jan 9. PMID:17258768
Page seeded by OCA on Wed Nov 21 09:45:06 2007
Categories: Escherichia coli | Single protein | Hong, S.B. | Lee, B.G. | Park, E.Y. | Song, H.K. | CA | PG4 | ZN | Treble cleft zinc finger
