Sandbox reserved 1754: Difference between revisions
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==RecA Protein Structure and Function== | ==RecA Protein Structure and Function== | ||
<StructureSection load='3cmx' size='340' side='right'caption='[[3cmx]], [[Resolution|resolution]] 2.70Å' scene='92/925552/5_monomers/ | <StructureSection load='3cmx' size='340' side='right'caption='[[3cmx]], [[Resolution|resolution]] 2.70Å' scene='92/925552/5_monomers/4'> | ||
== Monomer Structure == | == Monomer Structure == | ||
<scene name='92/925552/5_monomers/ | <scene name='92/925552/5_monomers/4'>RecA</scene> is one of the many proteins that is involved in recombination cross-over events and during recombination repair in response to single strand DNA breaks. RecA is a rather small monomer protein that can multiplex with itself up to thousands of RecA proteins to associate with ssDNA. The structure of RecA was determined through x-ray crystallography and each monomer contains very distinct structural components. These <scene name='92/925552/Reca_domains/4'>components</scene> are a largely helical 30-residue N-terminal region, a 240-residue α/ß ATPase core, and a 64-residue C-terminal | ||
RecA</scene> is one of the many proteins that is involved in recombination cross-over events and during recombination repair in response to single strand DNA breaks. RecA is a rather small monomer protein that can multiplex with itself up to thousands of RecA proteins to associate with ssDNA. The structure of RecA was determined through x-ray crystallography and each monomer contains very distinct structural components. These <scene name='92/925552/Reca_domains/4'>components</scene> are a largely helical 30-residue N-terminal region, a 240-residue α/ß ATPase core, and a 64-residue C-terminal | |||
globular domain. | globular domain. | ||
