2owl
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The DNA-binding protein, RdgC, is associated with recombination and | + | The DNA-binding protein, RdgC, is associated with recombination and replication fork repair in Escherichia coli and with the virulence-associated, pilin antigenic variation mediated by RecA and other recombination proteins in Neisseria species. We solved the structure of the E. coli protein and refined it to 2.4A. RdgC crystallizes as a dimer with a head-to-head, tail-to-tail organization forming a ring with a 30 A diameter hole at the center. The protein fold is unique and reminiscent of a horseshoe with twin gates closing the open end. The central hole is lined with positively charged residues and provides a highly plausible DNA binding channel consistent with the nonspecific mode of binding detected in vitro and with the ability of RdgC to modulate RecA function in vivo. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Ring | + | Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair., Briggs GS, McEwan PA, Yu J, Moore T, Emsley J, Lloyd RG, J Biol Chem. 2007 Apr 27;282(17):12353-7. Epub 2007 Feb 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17308310 17308310] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Briggs, G | + | [[Category: Briggs, G S.]] |
[[Category: Emsley, J.]] | [[Category: Emsley, J.]] | ||
| - | [[Category: Lloyd, R | + | [[Category: Lloyd, R G.]] |
| - | [[Category: McEwan, P | + | [[Category: McEwan, P A.]] |
[[Category: Moore, T.]] | [[Category: Moore, T.]] | ||
[[Category: Yu, J.]] | [[Category: Yu, J.]] | ||
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[[Category: replication]] | [[Category: replication]] | ||
| - | ''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 18:23:26 2008'' |
Revision as of 16:23, 21 February 2008
|
Crystal structure of E. coli RdgC
Overview
The DNA-binding protein, RdgC, is associated with recombination and replication fork repair in Escherichia coli and with the virulence-associated, pilin antigenic variation mediated by RecA and other recombination proteins in Neisseria species. We solved the structure of the E. coli protein and refined it to 2.4A. RdgC crystallizes as a dimer with a head-to-head, tail-to-tail organization forming a ring with a 30 A diameter hole at the center. The protein fold is unique and reminiscent of a horseshoe with twin gates closing the open end. The central hole is lined with positively charged residues and provides a highly plausible DNA binding channel consistent with the nonspecific mode of binding detected in vitro and with the ability of RdgC to modulate RecA function in vivo.
About this Structure
2OWL is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair., Briggs GS, McEwan PA, Yu J, Moore T, Emsley J, Lloyd RG, J Biol Chem. 2007 Apr 27;282(17):12353-7. Epub 2007 Feb 16. PMID:17308310
Page seeded by OCA on Thu Feb 21 18:23:26 2008
Categories: Escherichia coli | Single protein | Briggs, G S. | Emsley, J. | Lloyd, R G. | McEwan, P A. | Moore, T. | Yu, J. | CA | Reca | Recombination | Replication
