1urj

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==Overview==
==Overview==
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All organisms including animal viruses use specific proteins to bind, single-stranded DNA rapidly in a non-sequence-specific, flexible, and, cooperative manner during the DNA replication process. The crystal, structure of a 60-residue C-terminal deletion construct of ICP8, the major, single-stranded DNA-binding protein from herpes simplex virus-1, was, determined at 3.0 A resolution. The structure reveals a novel fold, consisting of a large N-terminal domain (residues 9-1038) and a small, C-terminal domain (residues 1049-1129). On the basis of the structure and, the nearest neighbor interactions in the crystal, we have presented a, model describing the site of single-stranded DNA binding and explaining, the basis for cooperative binding. This model agrees with the beaded, morphology observed in electron micrographs.
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All organisms including animal viruses use specific proteins to bind single-stranded DNA rapidly in a non-sequence-specific, flexible, and cooperative manner during the DNA replication process. The crystal structure of a 60-residue C-terminal deletion construct of ICP8, the major single-stranded DNA-binding protein from herpes simplex virus-1, was determined at 3.0 A resolution. The structure reveals a novel fold, consisting of a large N-terminal domain (residues 9-1038) and a small C-terminal domain (residues 1049-1129). On the basis of the structure and the nearest neighbor interactions in the crystal, we have presented a model describing the site of single-stranded DNA binding and explaining the basis for cooperative binding. This model agrees with the beaded morphology observed in electron micrographs.
==About this Structure==
==About this Structure==
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[[Category: Mapelli, M.]]
[[Category: Mapelli, M.]]
[[Category: Panjikar, S.]]
[[Category: Panjikar, S.]]
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[[Category: Tucker, P.A.]]
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[[Category: Tucker, P A.]]
[[Category: HG]]
[[Category: HG]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:04:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:31 2008''

Revision as of 13:27, 21 February 2008


1urj, resolution 3.0Å

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SINGLE STRANDED DNA-BINDING PROTEIN(ICP8) FROM HERPES SIMPLEX VIRUS-1

Overview

All organisms including animal viruses use specific proteins to bind single-stranded DNA rapidly in a non-sequence-specific, flexible, and cooperative manner during the DNA replication process. The crystal structure of a 60-residue C-terminal deletion construct of ICP8, the major single-stranded DNA-binding protein from herpes simplex virus-1, was determined at 3.0 A resolution. The structure reveals a novel fold, consisting of a large N-terminal domain (residues 9-1038) and a small C-terminal domain (residues 1049-1129). On the basis of the structure and the nearest neighbor interactions in the crystal, we have presented a model describing the site of single-stranded DNA binding and explaining the basis for cooperative binding. This model agrees with the beaded morphology observed in electron micrographs.

About this Structure

1URJ is a Single protein structure of sequence from Human herpesvirus 4 with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding., Mapelli M, Panjikar S, Tucker PA, J Biol Chem. 2005 Jan 28;280(4):2990-7. Epub 2004 Oct 26. PMID:15507432

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