Summary information and primary citation
- PDB-id
- 1rzt; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- transferase-DNA
- Method
- X-ray (2.1 Å)
- Summary
- Crystal structure of DNA polymerase lambda complexed with a two nucleotide gap DNA molecule
- Reference
- Garcia-Diaz M, Bebenek K, Krahn JM, Blanco L, Kunkel TA, Pedersen LC (2004): "A structural solution for the DNA polymerase lambda-dependent repair of DNA gaps with minimal homology." Mol.Cell, 13, 561-572. doi: 10.1016/S1097-2765(04)00061-9.
- Abstract
- Human DNA polymerase lambda (Pol lambda) is a family X member with low frameshift fidelity that has been suggested to perform gap-filling DNA synthesis during base excision repair and during repair of broken ends with limited homology. Here, we present a 2.1 A crystal structure of the catalytic core of Pol lambda in complex with DNA containing a two nucleotide gap. Pol lambda makes limited contacts with the template strand at the polymerase active site, and superimposition with Pol beta in a ternary complex suggests a shift in the position of the DNA at the active site that is reminiscent of a deletion intermediate. Surprisingly, Pol lambda can adopt a closed conformation, even in the absence of dNTP binding. These observations have implications for the catalytic mechanism and putative DNA repair functions of Pol lambda.
