1txy
From Proteopedia
(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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| - | [[Image:1txy.gif|left|200px]]<br /><applet load="1txy" size=" | + | [[Image:1txy.gif|left|200px]]<br /><applet load="1txy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1txy, resolution 2.00Å" /> | caption="1txy, resolution 2.00Å" /> | ||
'''E. coli PriB'''<br /> | '''E. coli PriB'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Maintenance of genome stability following DNA damage requires | + | 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== | ==About this Structure== | ||
| - | 1TXY 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:// | + | 1TXY 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=1TXY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Holton, J | + | [[Category: Holton, J M.]] |
| - | [[Category: Keck, J | + | [[Category: Keck, J L.]] |
[[Category: Lopper, M.]] | [[Category: Lopper, M.]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
[[Category: ob fold]] | [[Category: ob fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:30 2008'' |
Revision as of 13:18, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 15:18:30 2008
