2owy
From Proteopedia
(New page: 200px<br /><applet load="2owy" size="350" color="white" frame="true" align="right" spinBox="true" caption="2owy, resolution 2.500Å" /> '''The recombination-a...) |
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==Overview== | ==Overview== | ||
| - | RecA plays a central role in the nonmutagenic repair of stalled | + | RecA plays a central role in the nonmutagenic repair of stalled replication forks in bacteria. RdgC, a recombination-associated DNA-binding protein, is a potential negative regulator of RecA function. Here, we have determined the crystal structure of RdgC from Pseudomonas aeruginosa. The J-shaped monomer has a unique fold and can be divided into three structural domains: tip domain, center domain and base domain. Two such monomers dimerize to form a ring-shaped molecule of approximate 2-fold symmetry. Of the two inter-subunit interfaces within the dimer, one interface ('interface A') between tip/center domains is more nonpolar than the other ('interface B') between base domains. The structure allows us to propose that the RdgC dimer binds dsDNA through the central hole of approximately 30 A diameter. The proposed model is supported by our DNA-binding assays coupled with mutagenesis, which indicate that the conserved positively charged residues on the protein surface around the central hole play important roles in DNA binding. The novel ring-shaped architecture of the RdgC dimer has significant implications for its role in homologous recombination. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
[[Category: homologous recombination]] | [[Category: homologous recombination]] | ||
[[Category: pseudomonas aeruginosa]] | [[Category: pseudomonas aeruginosa]] | ||
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[[Category: ring-shaped dna binding proteins]] | [[Category: ring-shaped dna binding proteins]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:23:29 2008'' |
Revision as of 16:23, 21 February 2008
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The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding
Overview
RecA plays a central role in the nonmutagenic repair of stalled replication forks in bacteria. RdgC, a recombination-associated DNA-binding protein, is a potential negative regulator of RecA function. Here, we have determined the crystal structure of RdgC from Pseudomonas aeruginosa. The J-shaped monomer has a unique fold and can be divided into three structural domains: tip domain, center domain and base domain. Two such monomers dimerize to form a ring-shaped molecule of approximate 2-fold symmetry. Of the two inter-subunit interfaces within the dimer, one interface ('interface A') between tip/center domains is more nonpolar than the other ('interface B') between base domains. The structure allows us to propose that the RdgC dimer binds dsDNA through the central hole of approximately 30 A diameter. The proposed model is supported by our DNA-binding assays coupled with mutagenesis, which indicate that the conserved positively charged residues on the protein surface around the central hole play important roles in DNA binding. The novel ring-shaped architecture of the RdgC dimer has significant implications for its role in homologous recombination.
About this Structure
2OWY is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding., Ha JY, Kim HK, Kim do J, Kim KH, Oh SJ, Lee HH, Yoon HJ, Song HK, Suh SW, Nucleic Acids Res. 2007;35(8):2671-81. Epub 2007 Apr 10. PMID:17426134
Page seeded by OCA on Thu Feb 21 18:23:29 2008
