Summary information and primary citation
- PDB-id
-
1j1v;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- replication-DNA
- Method
- X-ray (2.1 Å)
- Summary
- Crystal structure of dnaa domainiv complexed with
dnaabox DNA
- Reference
-
Fujikawa N, Kurumizaka H, Nureki O, Terada T, Shirouzu M,
Katayama T, Yokoyama S (2003): "Structural
basis of replication origin recognition by the DnaA
protein." NUCLEIC ACIDS RES.,
31, 2077-2086. doi: 10.1093/nar/gkg309.
- Abstract
- Escherichia coli DnaA binds to 9 bp sequences (DnaA
boxes) in the replication origin, oriC, to form a complex
initiating chromosomal DNA replication. In the present
study, we determined the crystal structure of its
DNA-binding domain (domain IV) complexed with a DnaA box at
2.1 A resolution. DnaA domain IV contains a
helix-turn-helix motif for DNA binding. One helix and a
loop of the helix- turn-helix motif are inserted into the
major groove and 5 bp (3' two-thirds of the DnaA box
sequence) are recognized through base-specific hydrogen
bonds and van der Waals contacts with the C5-methyl groups
of thymines. In the minor groove, Arg399, located in the
loop adjacent to the motif, recognizes three more base
pairs (5' one-third of the DnaA box sequence) by
base-specific hydrogen bonds. DNA bending by approximately
28 degrees was also observed in the complex. These
base-specific interactions explain how DnaA exhibits higher
affinity for the strong DnaA boxes (R1, R2 and R4) than the
weak DnaA boxes (R3 and M) in the replication origin.