The crystal structure of Dps, a ferritin homolog that binds and protects DNA
The crystal structure of Dps, a DNA-binding protein from starved E. coli that protects DMA from oxidative damage, has been solved at 1.6 Å resolution. The Dps monomer has essentially the same fold as ferritin, which forms a 24-mer with 432 symmetry, a hollow core and pores at the three-fold axes. Dp...
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| Veröffentlicht in: | Nature Structural Biology 1998-04, Vol.5 (4), p.294-303 |
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| container_title | Nature Structural Biology |
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| creator | Grant, R.A. Filman, D.J. Finkel, S.E. Kolter, R. Hogle, J.M. |
| description | The crystal structure of Dps, a DNA-binding protein from starved
E. coli
that protects DMA from oxidative damage, has been solved at 1.6 Å resolution. The Dps monomer has essentially the same fold as ferritin, which forms a 24-mer with 432 symmetry, a hollow core and pores at the three-fold axes. Dps forms a dodecamer with 23 (tetrahedral) point group symmetry which also has a hollow core and pores at the three-folds. The structure suggests a novel DNA-binding motif and a mechanism for DNA protection based on the sequestration of Fe ions. |
| doi_str_mv | 10.1038/nsb0498-294 |
| format | Article |
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E. coli
that protects DMA from oxidative damage, has been solved at 1.6 Å resolution. The Dps monomer has essentially the same fold as ferritin, which forms a 24-mer with 432 symmetry, a hollow core and pores at the three-fold axes. Dps forms a dodecamer with 23 (tetrahedral) point group symmetry which also has a hollow core and pores at the three-folds. The structure suggests a novel DNA-binding motif and a mechanism for DNA protection based on the sequestration of Fe ions.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Crystallography, X-Ray</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - physiology</subject><subject>Ferritins - chemistry</subject><subject>Life Sciences</subject><subject>Macromolecular Substances</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Oxidative Stress</subject><subject>Point Mutation</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure</subject><subject>Protein Structure, Secondary</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><issn>1072-8368</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkL1PAyEYh4nR1FqdnE2YXOwpcHDAaFq_kkaXOhPguPaa-6jADf3vxfTiZOLEm_yePCQPANcY3WOUi4cuGESlyIikJ2CKGWWZlIKdphtxkom8EOfgIoQdQoQxnk_ARDJaEIKnYLXeOmj9IUTdwBD9YOPgHewruNyHOdSwct7Xse7gtm_7pt_AuNURmrorA9RdCfe-j87GAJfvj5fgrNJNcFfjOwOfz0_rxWu2-nh5WzyuMpszErNCMmsqIrQtLLGaYFFIV_GCYmycQYYaIgzjjErLtRMl5rhwRvNcIEu44_kM3B696fOvwYWo2jpY1zS6c_0QFJdcpiL_g8mMBSUsgXdH0Po-BO8qtfd1q_1BYaR-IqsxskqRE30zagfTuvKXHaumfX7cQ1q6jfNq1w--S0n-1H0DKgmFgw</recordid><startdate>19980401</startdate><enddate>19980401</enddate><creator>Grant, R.A.</creator><creator>Filman, D.J.</creator><creator>Finkel, S.E.</creator><creator>Kolter, R.</creator><creator>Hogle, J.M.</creator><general>Nature Publishing Group US</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19980401</creationdate><title>The crystal structure of Dps, a ferritin homolog that binds and protects DNA</title><author>Grant, R.A. ; 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E. coli
that protects DMA from oxidative damage, has been solved at 1.6 Å resolution. The Dps monomer has essentially the same fold as ferritin, which forms a 24-mer with 432 symmetry, a hollow core and pores at the three-fold axes. Dps forms a dodecamer with 23 (tetrahedral) point group symmetry which also has a hollow core and pores at the three-folds. The structure suggests a novel DNA-binding motif and a mechanism for DNA protection based on the sequestration of Fe ions.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>9546221</pmid><doi>10.1038/nsb0498-294</doi><tpages>10</tpages></addata></record> |
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| ispartof | Nature Structural Biology, 1998-04, Vol.5 (4), p.294-303 |
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| language | eng |
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| source | MEDLINE; Nature Journals Online; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences Crystallography, X-Ray DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Escherichia coli Escherichia coli - physiology Ferritins - chemistry Life Sciences Macromolecular Substances Membrane Biology Models, Molecular Molecular Sequence Data Oxidative Stress Point Mutation Protein Conformation Protein Folding Protein Structure Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid |
| title | The crystal structure of Dps, a ferritin homolog that binds and protects DNA |
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