1aa3
From Proteopedia
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| - | [[Image:1aa3.gif|left|200px]] | + | [[Image:1aa3.gif|left|200px]] |
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| - | '''C-TERMINAL DOMAIN OF THE E. COLI RECA, NMR, MINIMIZED AVERAGE STRUCTURE''' | + | {{Structure |
| + | |PDB= 1aa3 |SIZE=350|CAPTION= <scene name='initialview01'>1aa3</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''C-TERMINAL DOMAIN OF THE E. COLI RECA, NMR, MINIMIZED AVERAGE STRUCTURE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AA3 is a [ | + | 1AA3 is a [[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=1AA3 OCA]. |
==Reference== | ==Reference== | ||
| - | An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing., Aihara H, Ito Y, Kurumizaka H, Terada T, Yokoyama S, Shibata T, J Mol Biol. 1997 Nov 28;274(2):213-21. PMID:[http:// | + | An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing., Aihara H, Ito Y, Kurumizaka H, Terada T, Yokoyama S, Shibata T, J Mol Biol. 1997 Nov 28;274(2):213-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9398528 9398528] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:55:05 2008'' |
Revision as of 07:55, 20 March 2008
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C-TERMINAL DOMAIN OF THE E. COLI RECA, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
RecA protein and its homologs catalyze homologous pairing of dsDNA and ssDNA, a critical reaction in homologous genetic recombination in various organisms from a virus, microbes to higher eukaryotes. In this reaction, RecA protein forms a nucleoprotein filament on ssDNA, which in turn binds to naked dsDNA for homology search. We suggested that the C-terminal domain of RecA protein plays a role in capturing the dsDNA. Here, we isolated the C-terminal domain as a soluble form and determined the solution structure by NMR spectroscopy. The overall folding of the NMR structure agrees with that of the corresponding part of the reported crystal structure, but a remarkable difference was found in a solvent-exposed region due to intermolecular contacts in the crystal. Then, we studied the interaction between the C-terminal domain and DNA, and found that significant chemical shift changes were induced in a specific region by titration with dsDNA. SsDNA induced a much smaller chemical shift perturbation. The difference of DNA concentrations to give the half-saturation of the chemical shift change showed a higher affinity of the C-terminal region toward dsDNA. Combined with our previous results, these provide direct evidence that the defined region in the C-terminal domain furnishes a binding surface for DNA.
About this Structure
1AA3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing., Aihara H, Ito Y, Kurumizaka H, Terada T, Yokoyama S, Shibata T, J Mol Biol. 1997 Nov 28;274(2):213-21. PMID:9398528
Page seeded by OCA on Thu Mar 20 09:55:05 2008
