The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding

Marina Mapelli, Santosh Panjikar, Paul A. Tucker

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)2990-2997
Number of pages8
JournalJournal of Biological Chemistry
Volume280
Issue number4
DOIs
Publication statusPublished - Jan 28 2005

Fingerprint

Single-Stranded DNA
Human Herpesvirus 1
Viruses
Carrier Proteins
Crystal structure
DNA-Binding Proteins
DNA Replication
Animals
Electrons
Crystals
DNA
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding. / Mapelli, Marina; Panjikar, Santosh; Tucker, Paul A.

In: Journal of Biological Chemistry, Vol. 280, No. 4, 28.01.2005, p. 2990-2997.

Research output: Contribution to journalArticle

@article{fa43acbc1cb14049b1bf766d6494117d,
title = "The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding",
abstract = "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.",
author = "Marina Mapelli and Santosh Panjikar and Tucker, {Paul A.}",
year = "2005",
month = "1",
day = "28",
doi = "10.1074/jbc.M406780200",
language = "English",
volume = "280",
pages = "2990--2997",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "4",

}

TY - JOUR

T1 - The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding

AU - Mapelli, Marina

AU - Panjikar, Santosh

AU - Tucker, Paul A.

PY - 2005/1/28

Y1 - 2005/1/28

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=13244284795&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=13244284795&partnerID=8YFLogxK

U2 - 10.1074/jbc.M406780200

DO - 10.1074/jbc.M406780200

M3 - Article

C2 - 15507432

AN - SCOPUS:13244284795

VL - 280

SP - 2990

EP - 2997

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 4

ER -