1o7i
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Information processing pathways such as DNA replication are conserved in, eukaryotes and archaea and are significantly different from those found in, bacteria. Single-stranded DNA-binding (SSB) proteins (or replication, protein A, RPA, in eukaryotes) play a central role in many of these, pathways. However, whilst euryarchaea have a eukaryotic-type RPA, homologue, crenarchaeal SSB proteins appear much more similar to the, bacterial proteins, with a single OB fold for DNA binding and a flexible, C-terminal tail that is implicated in protein-protein interactions. We, have determined the crystal structure of the SSB protein from the, crenarchaeote Sulfolobus solfataricus to 1.26 A. The structure shows a, striking and unexpected similarity to the DNA-binding domains of human, RPA, providing .. | + | Information processing pathways such as DNA replication are conserved in, eukaryotes and archaea and are significantly different from those found in, bacteria. Single-stranded DNA-binding (SSB) proteins (or replication, protein A, RPA, in eukaryotes) play a central role in many of these, pathways. However, whilst euryarchaea have a eukaryotic-type RPA, homologue, crenarchaeal SSB proteins appear much more similar to the, bacterial proteins, with a single OB fold for DNA binding and a flexible, C-terminal tail that is implicated in protein-protein interactions. We, have determined the crystal structure of the SSB protein from the, crenarchaeote Sulfolobus solfataricus to 1.26 A. The structure shows a, striking and unexpected similarity to the DNA-binding domains of human, RPA, providing confirmation of the close relationship between archaea and, eukaryotes. The high resolution of the structure, together with, thermodynamic and mutational studies of DNA binding, allow us to propose a, molecular basis for DNA binding and define the features required for, eukaryotic and archaeal OB folds. |
==About this Structure== | ==About this Structure== | ||
| - | 1O7I is a | + | 1O7I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O7I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: single stranded dna]] | [[Category: single stranded dna]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:11:55 2007'' |
Revision as of 13:06, 5 November 2007
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CRYSTAL STRUCTURE OF A SINGLE STRANDED DNA BINDING PROTEIN
Overview
Information processing pathways such as DNA replication are conserved in, eukaryotes and archaea and are significantly different from those found in, bacteria. Single-stranded DNA-binding (SSB) proteins (or replication, protein A, RPA, in eukaryotes) play a central role in many of these, pathways. However, whilst euryarchaea have a eukaryotic-type RPA, homologue, crenarchaeal SSB proteins appear much more similar to the, bacterial proteins, with a single OB fold for DNA binding and a flexible, C-terminal tail that is implicated in protein-protein interactions. We, have determined the crystal structure of the SSB protein from the, crenarchaeote Sulfolobus solfataricus to 1.26 A. The structure shows a, striking and unexpected similarity to the DNA-binding domains of human, RPA, providing confirmation of the close relationship between archaea and, eukaryotes. The high resolution of the structure, together with, thermodynamic and mutational studies of DNA binding, allow us to propose a, molecular basis for DNA binding and define the features required for, eukaryotic and archaeal OB folds.
About this Structure
1O7I is a Single protein structure of sequence from Sulfolobus solfataricus with SO4 as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein., Kerr ID, Wadsworth RI, Cubeddu L, Blankenfeldt W, Naismith JH, White MF, EMBO J. 2003 Jun 2;22(11):2561-70. PMID:12773373
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