Snapshots of RecA Protein Involving Movement of the C-domain and Different Conformations of the DNA-binding Loops: Crystallographic and Comparative Analysis of 11 Structures of Mycobacterium smegmatis RecA

Mycobacterium smegmatis RecA and its nucleotide complexes crystallize in three different, but closely related, forms characterized by specific ranges of unit cell dimensions. The six crystals reported here and five reported earlier, all grown under the same or very similar conditions, belong to thes...

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Veröffentlicht in:	Journal of molecular biology 2007-04, Vol.367 (4), p.1130-1144
Hauptverfasser:	Krishna, R., Prabu, J. Rajan, Manjunath, G.P., Datta, S., Chandra, N.R., Muniyappa, K., Vijayan, M.
Format:	Artikel
Sprache:	eng
Schlagworte:	ATP-binding Binding Sites Crystallography, X-Ray DNA-binding DNA-Binding Proteins - chemistry Escherichia coli Glycine - chemistry Models, Molecular Mycobacterium smegmatis Mycobacterium smegmatis - enzymology Protein Conformation Protein Folding Protein Structure, Tertiary Rec A Recombinases - chemistry Rec A Recombinases - classification recombination repair SOS response
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