1U98
Crystal Structure of E. coli RecA in a Compressed Helical Filament Form3
Summary for 1U98
| Entry DOI | 10.2210/pdb1u98/pdb |
| Related | 1U94 |
| Descriptor | RecA protein, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | reca, homologous recombination, atpase, dna repair, dna binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 38578.81 |
| Authors | Xing, X.,Bell, C.E. (deposition date: 2004-08-09, release date: 2004-09-21, Last modification date: 2023-08-23) |
| Primary citation | Xing, X.,Bell, C.E. Crystal structures of Escherichia coli RecA in a compressed helical filament. J.Mol.Biol., 342:1471-1485, 2004 Cited by PubMed Abstract: The X-ray crystal structure of uncomplexed Escherichia coli RecA protein has been determined in three new crystal forms at resolutions of 1.9 A, 2.0 A, and 2.6 A. The RecA protein used for this study contains the extra residues Gly-Ser-His-Met at the N terminus, but retains normal ssDNA-dependent ATPase and coprotease activities. In all three crystals, RecA is packed in a right-handed helical filament with a pitch of approximately 74 A. These RecA filaments are compressed relative to the original crystal structure of RecA, which has a helical pitch of 82.7 A. In the structures of the compressed RecA filament, the monomer-monomer interface and the core domain are essentially the same as in the RecA structure with the 83 A pitch. The change in helical pitch is accommodated by a small movement of the N-terminal domain, which is reoriented to preserve the contacts it makes at the monomer-monomer interface. The new crystal structures show significant variation in the orientation and conformation of the C-terminal domain, as well as in the inter-filament packing interactions. In crystal form 2, a calcium ion is bound closely to a beta-hairpin of the C-terminal domain and to Asp38 of a neighboring filament, and residues 329-331 of the C-terminal tail become ordered to contact a neighboring filament. In crystal forms 3 and 4, a sulfate ion or a phosphate anion is bound to the same site on RecA as the beta-phosphate group of ADP, causing an opening of the P-loop. Altogether, the structures show the conformational variability of RecA protein in the crystalline state, providing insight into many aspects of RecA function. PubMed: 15364575DOI: 10.1016/j.jmb.2004.07.091 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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