1PJR
STRUCTURE OF DNA HELICASE
Summary for 1PJR
| Entry DOI | 10.2210/pdb1pjr/pdb |
| Descriptor | PCRA (2 entities in total) |
| Functional Keywords | dna repair, dna replication, sos response, helicase, atp-binding, dna-binding |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 82595.10 |
| Authors | Subramanya, H.S.,Bird, L.E.,Brannigan, J.A.,Wigley, D.B. (deposition date: 1996-10-11, release date: 1997-12-03, Last modification date: 2024-02-14) |
| Primary citation | Subramanya, H.S.,Bird, L.E.,Brannigan, J.A.,Wigley, D.B. Crystal structure of a DExx box DNA helicase. Nature, 384:379-383, 1996 Cited by PubMed Abstract: There are a wide variety of helicases that unwind helical DNA and RNA substrates. The twelve helicases that have been identified in Escherichia coli play a role in almost all cellular processes involving nucleic acids. We have solved the crystal structure of a monomeric form of a DNA helicase from Bacillus stearothermophilus, alone and in a complex with ADP, at 2.5 and 2.9 A resolution, respectively. The enzyme comprises two domains with a deep cleft running between them. The ATP-binding site, which is situated at the bottom of this cleft, is formed by motifs that are conserved across the superfamily of related helicases. Unexpected structural homology with the DNA recombination protein, RecA, suggests how ATP binding and hydrolysis may drive conformational changes of the enzyme during catalysis, and implies that there is a common mechanism for all helicases. PubMed: 8934527DOI: 10.1038/384379a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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