2ccz: Difference between revisions

Line 4:

==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.

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==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Hsiao, C.D.]]

[[Category: Hsiao, C D.]]

[[Category: Hsu, C.H.]]

[[Category: Hsu, C H.]]

[[Category: Huang, C.Y.]]

[[Category: Huang, C Y.]]

[[Category: Sun, Y.J.]]

[[Category: Sun, Y J.]]

[[Category: Wu, H.N.]]

[[Category: Wu, H N.]]

[[Category: dna recombination]]

[[Category: dna repair]]

Line 27:

[[Category: ssdna]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 14~~:57:14 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:26 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Hsiao, C.D.]]
+[[Category: Hsiao, C D.]]
-[[Category: Hsu, C.H.]]
+[[Category: Hsu, C H.]]
-[[Category: Huang, C.Y.]]
+[[Category: Huang, C Y.]]
-[[Category: Sun, Y.J.]]
+[[Category: Sun, Y J.]]
-[[Category: Wu, H.N.]]
+[[Category: Wu, H N.]]
 [[Category: dna recombination]]
 [[Category: dna repair]]
@@ Line 27: / Line 27: @@
 [[Category: ssdna]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:57:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:26 2008''