2REB
THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER
Summary for 2REB
Entry DOI | 10.2210/pdb2reb/pdb |
Descriptor | REC A (2 entities in total) |
Functional Keywords | self-cleavage stimulation, homologous recombination, dna binding protein |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A7G6 |
Total number of polymer chains | 1 |
Total formula weight | 37885.09 |
Authors | Story, R.M.,Steitz, T.A. (deposition date: 1992-03-06, release date: 1993-10-31, Last modification date: 2024-02-21) |
Primary citation | Story, R.M.,Weber, I.T.,Steitz, T.A. The structure of the E. coli recA protein monomer and polymer. Nature, 355:318-325, 1992 Cited by PubMed Abstract: The crystal structure of the recA protein from Escherichia coli at 2.3-A resolution reveals a major domain that binds ADP and probably single- and double-stranded DNA. Two smaller subdomains at the N and C termini protrude from the protein and respectively stabilize a 6(1) helical polymer of protein subunits and interpolymer bundles. This polymer structure closely resembles that of recA/DNA filaments determined by electron microscopy. Mutations in recA protein that enhance coprotease, DNA-binding and/or strand-exchange activity can be explained if the interpolymer interactions in the crystal reflect a regulatory mechanism in vivo. PubMed: 1731246DOI: 10.1038/355318a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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