1woc: Difference between revisions

Revision as of 16:46, 21 February 2008

Crystal structure of PriB

OverviewOverview

PriB is not only an essential protein necessary for the replication restart on the collapsed and disintegrated replication fork, but also an important protein for assembling of primosome onto PhiX174 genomic DNA during replication initiation. Here we report a 2.0-A-resolution X-ray structure of a biologically functional form of PriB from Escherichia coli. The crystal structure revealed that despite a low level of primary sequence identity, the PriB monomer, as well as the dimeric form, are structurally identical to the N-terminal DNA-binding domain of the single-stranded DNA-binding protein (SSB) from Escherichia coli, which possesses an oligonucleotides-binding-fold. The oligonucleotide-PriB complex model based on the oligonucleotides-SSB complex structure suggested that PriB had a DNA-binding pocket conserved in SSB from Escherichia coli and might bind to single-stranded DNA in the manner of SSB. Furthermore, surface plasmon resonance analysis and fluorescence measurements demonstrated that PriB binds single-stranded DNA with high affinity, by involving tryptophan residue. The significance of these results with respect to the functional role of PriB in the assembly of primosome is discussed.

About this StructureAbout this Structure

1WOC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site., Shioi S, Ose T, Maenaka K, Shiroishi M, Abe Y, Kohda D, Katayama T, Ueda T, Biochem Biophys Res Commun. 2005 Jan 28;326(4):766-76. PMID:15607735

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-[[Image:1woc.gif|left|200px]]<br /><applet load="1woc" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1woc, resolution 2.&Aring;" />
 '''Crystal structure of PriB'''<br />
 ==Overview==
-PriB is not only an essential protein necessary for the replication, restart on the collapsed and disintegrated replication fork, but also an, important protein for assembling of primosome onto PhiX174 genomic DNA, during replication initiation. Here we report a 2.0-A-resolution X-ray, structure of a biologically functional form of PriB from Escherichia coli., The crystal structure revealed that despite a low level of primary, sequence identity, the PriB monomer, as well as the dimeric form, are, structurally identical to the N-terminal DNA-binding domain of the, single-stranded DNA-binding protein (SSB) from Escherichia coli, which, possesses an oligonucleotides-binding-fold. The oligonucleotide-PriB, complex model based on the oligonucleotides-SSB complex structure, suggested that PriB had a DNA-binding pocket conserved in SSB from, Escherichia coli and might bind to single-stranded DNA in the manner of, SSB. Furthermore, surface plasmon resonance analysis and fluorescence, measurements demonstrated that PriB binds single-stranded DNA with high, affinity, by involving tryptophan residue. The significance of these, results with respect to the functional role of PriB in the assembly of, primosome is discussed.
+PriB is not only an essential protein necessary for the replication restart on the collapsed and disintegrated replication fork, but also an important protein for assembling of primosome onto PhiX174 genomic DNA during replication initiation. Here we report a 2.0-A-resolution X-ray structure of a biologically functional form of PriB from Escherichia coli. The crystal structure revealed that despite a low level of primary sequence identity, the PriB monomer, as well as the dimeric form, are structurally identical to the N-terminal DNA-binding domain of the single-stranded DNA-binding protein (SSB) from Escherichia coli, which possesses an oligonucleotides-binding-fold. The oligonucleotide-PriB complex model based on the oligonucleotides-SSB complex structure suggested that PriB had a DNA-binding pocket conserved in SSB from Escherichia coli and might bind to single-stranded DNA in the manner of SSB. Furthermore, surface plasmon resonance analysis and fluorescence measurements demonstrated that PriB binds single-stranded DNA with high affinity, by involving tryptophan residue. The significance of these results with respect to the functional role of PriB in the assembly of primosome is discussed.
 ==About this Structure==
-WOC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WOC OCA].
+WOC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOC OCA].
 ==Reference==
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 [[Category: oligonucleotide binding fold]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:29 2008''