2ccz

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==Overview==
==Overview==
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PriB is a primosomal protein required for replication restart in, Escherichia coli. PriB stimulates PriA helicase activity via interaction, with single-stranded DNA (ssDNA), but the molecular details of this, interaction remain unclear. Here, we report the crystal structure of PriB, complexed with a 15 bases oligonucleotide (dT15) at 2.7 A resolution. PriB, shares structural similarity with the E.coli ssDNA-binding protein, (EcoSSB). However, the structure of the PriB-dT15 complex reveals that, PriB binds ssDNA differently. Results from filter-binding assays show that, PriB-ssDNA interaction is salt-sensitive and cooperative. Mutational, analysis suggests that the loop L45 plays an important role in ssDNA, binding. Based on the crystal structure and biochemical analyses, we, propose a cooperative mechanism for the binding of PriB to ssDNA and a, model for the assembly of the PriA-PriB-ssDNA complex. This report, presents the first structure of a replication restart primosomal protein, complexed with DNA, and a novel model that explains the interactions, between a dimeric oligonucleotide-binding-fold protein and ssDNA.
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PriB is a primosomal protein required for replication restart in Escherichia coli. PriB stimulates PriA helicase activity via interaction with single-stranded DNA (ssDNA), but the molecular details of this interaction remain unclear. Here, we report the crystal structure of PriB complexed with a 15 bases oligonucleotide (dT15) at 2.7 A resolution. PriB shares structural similarity with the E.coli ssDNA-binding protein (EcoSSB). However, the structure of the PriB-dT15 complex reveals that PriB binds ssDNA differently. Results from filter-binding assays show that PriB-ssDNA interaction is salt-sensitive and cooperative. Mutational analysis suggests that the loop L45 plays an important role in ssDNA binding. Based on the crystal structure and biochemical analyses, we propose a cooperative mechanism for the binding of PriB to ssDNA and a model for the assembly of the PriA-PriB-ssDNA complex. This report presents the first structure of a replication restart primosomal protein complexed with DNA, and a novel model that explains the interactions between a dimeric oligonucleotide-binding-fold protein and ssDNA.
==About this Structure==
==About this Structure==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hsiao, C.D.]]
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[[Category: Hsiao, C D.]]
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[[Category: Hsu, C.H.]]
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[[Category: Hsu, C H.]]
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[[Category: Huang, C.Y.]]
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[[Category: Huang, C Y.]]
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[[Category: Sun, Y.J.]]
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[[Category: Sun, Y J.]]
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[[Category: Wu, H.N.]]
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[[Category: Wu, H N.]]
[[Category: dna recombination]]
[[Category: dna recombination]]
[[Category: dna repair]]
[[Category: dna repair]]
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[[Category: ssdna]]
[[Category: ssdna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:57:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:26 2008''

Revision as of 14:47, 21 February 2008


2ccz, resolution 2.70Å

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CRYSTAL STRUCTURE OF E. COLI PRIMOSOMOL PROTEIN PRIB BOUND TO SSDNA

Overview

PriB is a primosomal protein required for replication restart in Escherichia coli. PriB stimulates PriA helicase activity via interaction with single-stranded DNA (ssDNA), but the molecular details of this interaction remain unclear. Here, we report the crystal structure of PriB complexed with a 15 bases oligonucleotide (dT15) at 2.7 A resolution. PriB shares structural similarity with the E.coli ssDNA-binding protein (EcoSSB). However, the structure of the PriB-dT15 complex reveals that PriB binds ssDNA differently. Results from filter-binding assays show that PriB-ssDNA interaction is salt-sensitive and cooperative. Mutational analysis suggests that the loop L45 plays an important role in ssDNA binding. Based on the crystal structure and biochemical analyses, we propose a cooperative mechanism for the binding of PriB to ssDNA and a model for the assembly of the PriA-PriB-ssDNA complex. This report presents the first structure of a replication restart primosomal protein complexed with DNA, and a novel model that explains the interactions between a dimeric oligonucleotide-binding-fold protein and ssDNA.

About this Structure

2CCZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode., Huang CY, Hsu CH, Sun YJ, Wu HN, Hsiao CD, Nucleic Acids Res. 2006;34(14):3878-86. Epub 2006 Aug 9. PMID:16899446

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