1txy
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(New page: 200px<br /><applet load="1txy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1txy, resolution 2.00Å" /> '''E. coli PriB'''<br /...)
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Revision as of 01:33, 21 November 2007
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E. coli PriB
Overview
Maintenance of genome stability following DNA damage requires, origin-independent reinitiation of DNA replication at repaired replication, forks. In E. coli, PriA, PriB, PriC, and DnaT play critical roles in, recognizing repaired replication forks and reloading the replisome onto, the template to reinitiate DNA replication. Here, we report the 2.0 A, resolution crystal structure of E. coli PriB, revealing a dimer that, consists of a single structural domain formed by two, oligonucleotide/oligosaccharide binding (OB) folds. Structural similarity, of PriB to single-stranded DNA binding proteins reveals insights into its, mechanisms of DNA binding. The structure further establishes a putative, protein interaction surface that may contribute to the role of PriB in, primosome assembly by facilitating interactions with PriA and DnaT. This, is the first high-resolution structure of a protein involved in, oriC-independent replisome loading and provides unique insight into, mechanisms of replication restart in E. coli.
About this Structure
1TXY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of PriB, a component of the Escherichia coli replication restart primosome., Lopper M, Holton JM, Keck JL, Structure. 2004 Nov;12(11):1967-75. PMID:15530361
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