1iz5
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(New page: 200px<br /><applet load="1iz5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iz5, resolution 1.80Å" /> '''Pyrococcus furiosus ...)
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Revision as of 15:40, 20 November 2007
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Pyrococcus furiosus PCNA mutant (Met73Leu, Asp143Ala, Asp147Ala): orthorhombic form
Overview
Two mutant proliferating cell nuclear antigens from the hyperthermophilic, archaeon Pyrococcus furiosus, PfuPCNA(D143A) and PfuPCNA(D143A/D147A), were prepared by site-specific mutagenesis. The results from gel, filtration showed that mutations at D143 and D147 drastically affect the, stability of the trimeric structure of PfuPCNA. The PfuPCNA(D143A) still, retained the activity to stimulate the DNA polymerase reaction, but, PfuPCNA(D143A/D147A) lost the activity. Crystal structures of the mutant, PfuPCNAs were determined. Although the wild-type PCNA forms a toroidal, trimer with intermolecular hydrogen bonds between the N- and C-terminal, domains, the mutant PfuPCNAs exist as V-shaped dimers through, intermolecular hydrogen bonds between the two C-terminal domains in the, crystal. Because the mutated residues are involved in the intermolecular, ion pairs through their side chains in the wild-type PfuPCNA, these ion, pairs seem to play a key role in maintaining the toroidal structure of the, PfuPCNA trimer. The comparison of the crystal structures revealed, intriguing conformational flexibility of each domain in the PfuPCNA, subunit. This structural versatility of PCNA may be involved in the, mechanisms for ring opening and closing.
About this Structure
1IZ5 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
Intermolecular ion pairs maintain the toroidal structure of Pyrococcus furiosus PCNA., Matsumiya S, Ishino S, Ishino Y, Morikawa K, Protein Sci. 2003 Apr;12(4):823-31. PMID:12649440
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