1woc
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(New page: 200px<br /><applet load="1woc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1woc, resolution 2.Å" /> '''Crystal structure of P...)
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Revision as of 03:26, 21 November 2007
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Crystal structure of PriB
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.
About this Structure
1WOC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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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