1em8
From Proteopedia
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'''Crystal structure of chi and psi subunit heterodimer from DNA POL III''' | '''Crystal structure of chi and psi subunit heterodimer from DNA POL III''' | ||
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[[Category: Gulbis, J M.]] | [[Category: Gulbis, J M.]] | ||
[[Category: Kuriyan, J.]] | [[Category: Kuriyan, J.]] | ||
| - | [[Category: | + | [[Category: Alpha-beta fold]] |
| - | [[Category: | + | [[Category: Clamp-loader]] |
| - | [[Category: | + | [[Category: Dna pol iii]] |
| - | [[Category: | + | [[Category: Heterodimer]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:16:12 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:16, 2 May 2008
Crystal structure of chi and psi subunit heterodimer from DNA POL III
Overview
The chi (chi) and psi (psi) subunits of Escherichia coli DNA polymerase III form a heterodimer that is associated with the ATP-dependent clamp-loader machinery. In E. coli, the chi:psi heterodimer serves as a bridge between the clamp-loader complex and the single-stranded DNA-binding protein. We determined the crystal structure of the chi:psi heterodimer at 2.1 A resolution. Although neither chi (147 residues) nor psi (137 residues) bind to nucleotides, the fold of each protein is similar to the folds of mononucleotide-(chi) or dinucleotide-(psi) binding proteins, without marked similarity to the structures of the clamp-loader subunits. Genes encoding chi and psi proteins are found to be readily identifiable in several bacterial genomes and sequence alignments showed that residues at the chi:psi interface are highly conserved in both proteins, suggesting that the heterodimeric interaction is of functional significance. The conservation of surface-exposed residues is restricted to the interfacial region and to just two other regions in the chi:psi complex. One of the conserved regions was found to be located on chi, distal to the psi interaction region, and we identified this as the binding site for a C-terminal segment of the single-stranded DNA-binding protein. The other region of sequence conservation is localized to an N-terminal segment of psi (26 residues) that is disordered in the crystal structure. We speculate that psi is linked to the clamp-loader complex by this flexible, but conserved, N-terminal segment, and that the chi:psi unit is linked to the single-stranded DNA-binding protein via the distal surface of chi. The base of the clamp-loader complex has an open C-shaped structure, and the shape of the chi:psi complex is suggestive of a loose docking within the crevice formed by the open faces of the delta and delta' subunits of the clamp-loader.
About this Structure
1EM8 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the chi:psi sub-assembly of the Escherichia coli DNA polymerase clamp-loader complex., Gulbis JM, Kazmirski SL, Finkelstein J, Kelman Z, O'Donnell M, Kuriyan J, Eur J Biochem. 2004 Jan;271(2):439-49. PMID:14717711 Page seeded by OCA on Fri May 2 15:16:12 2008
