1rep
From Proteopedia
(New page: 200px<br /><applet load="1rep" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rep, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1rep.gif|left|200px]]<br /><applet load="1rep" size=" | + | [[Image:1rep.gif|left|200px]]<br /><applet load="1rep" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rep, resolution 2.6Å" /> | caption="1rep, resolution 2.6Å" /> | ||
'''CRYSTAL STRUCTURE OF REPLICATION INITIATOR PROTEIN REPE54 OF MINI-F PLASMID COMPLEXED WITH AN ITERON DNA'''<br /> | '''CRYSTAL STRUCTURE OF REPLICATION INITIATOR PROTEIN REPE54 OF MINI-F PLASMID COMPLEXED WITH AN ITERON DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The initiator protein (RepE) of F factor, a plasmid involved in sexual | + | The initiator protein (RepE) of F factor, a plasmid involved in sexual conjugation in Escherichia coli, has dual functions during the initiation of DNA replication which are determined by whether it exists as a dimer or as a monomer. A RepE monomer functions as a replication initiator, but a RepE dimer functions as an autogenous repressor. We have solved the crystal structure of the RepE monomer bound to an iteron DNA sequence of the replication origin of plasmid F. The RepE monomer consists of topologically similar N- and C-terminal domains related to each other by internal pseudo 2-fold symmetry, despite the lack of amino acid similarities between the domains. Both domains bind to the two major grooves of the iteron (19 bp) with different binding affinities. The C-terminal domain plays the leading role in this binding, while the N-terminal domain has an additional role in RepE dimerization. The structure also suggests that superhelical DNA induced at the origin of plasmid F by four RepEs and one HU dimer has an essential role in the initiation of DNA replication. |
==About this Structure== | ==About this Structure== | ||
| - | 1REP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1REP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REP OCA]. |
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: replication initiator]] | [[Category: replication initiator]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:03 2008'' |
Revision as of 12:50, 21 February 2008
|
CRYSTAL STRUCTURE OF REPLICATION INITIATOR PROTEIN REPE54 OF MINI-F PLASMID COMPLEXED WITH AN ITERON DNA
Overview
The initiator protein (RepE) of F factor, a plasmid involved in sexual conjugation in Escherichia coli, has dual functions during the initiation of DNA replication which are determined by whether it exists as a dimer or as a monomer. A RepE monomer functions as a replication initiator, but a RepE dimer functions as an autogenous repressor. We have solved the crystal structure of the RepE monomer bound to an iteron DNA sequence of the replication origin of plasmid F. The RepE monomer consists of topologically similar N- and C-terminal domains related to each other by internal pseudo 2-fold symmetry, despite the lack of amino acid similarities between the domains. Both domains bind to the two major grooves of the iteron (19 bp) with different binding affinities. The C-terminal domain plays the leading role in this binding, while the N-terminal domain has an additional role in RepE dimerization. The structure also suggests that superhelical DNA induced at the origin of plasmid F by four RepEs and one HU dimer has an essential role in the initiation of DNA replication.
About this Structure
1REP is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a prokaryotic replication initiator protein bound to DNA at 2.6 A resolution., Komori H, Matsunaga F, Higuchi Y, Ishiai M, Wada C, Miki K, EMBO J. 1999 Sep 1;18(17):4597-607. PMID:10469640
Page seeded by OCA on Thu Feb 21 14:50:03 2008
