1RZT

Crystal structure of DNA polymerase lambda complexed with a two nucleotide gap DNA molecule

Summary for 1RZT

• Entry DOI: 10.2210/pdb1rzt/pdb
• Descriptor: 5'-D(*CP*GP*GP*CP*AP*AP*CP*GP*CP*AP*C)-3', 5'-D(*GP*TP*GP*CP*G)-3', 5'-D(P*GP*CP*CP*G)-3', ... (7 entities in total)
• Functional Keywords: dna polymerase lambda, transferase-dna complex, transferase/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q9UGP5
• Total number of polymer chains: 16
• Total formula weight: 172725.09

Authors

Pedersen, L.C.,Garcia-Diaz, M.,Bebenek, K.,Krahn, J.M.,Blanco, L.,Kunkel, T.A. (deposition date: 2003-12-29, release date: 2004-03-02, Last modification date: 2024-10-09)

Primary citation

Garcia-Diaz, M.,Bebenek, K.,Krahn, J.M.,Blanco, L.,Kunkel, T.A.,Pedersen, L.C.
A structural solution for the DNA polymerase lambda-dependent repair of DNA gaps with minimal homology.
Mol.Cell, 13:561-572, 2004

PubMed 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.

PubMed: 14992725
DOI: 10.1016/S1097-2765(04)00061-9

Experimental method

X-RAY DIFFRACTION (2.1 Å)