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PDBsum entry 1rzt

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Top Page protein dna_rna ligands metals Protein-protein interface(s) links
Transferase/DNA PDB id
1rzt
Contents
Protein chains
327 a.a. *
DNA/RNA
Ligands
EDO
Metals
_NA ×10
Waters ×1026
* Residue conservation analysis

References listed in PDB file
Key reference
Title A structural solution for the DNA polymerase lambda-Dependent repair of DNA gaps with minimal homology.
Authors M.Garcia-Diaz, K.Bebenek, J.M.Krahn, L.Blanco, T.A.Kunkel, L.C.Pedersen.
Ref. Mol Cell, 2004, 13, 561-572. [DOI no: 10.1016/S1097-2765(04)00061-9]
PubMed id 14992725
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.
Figure 4.
Figure 4. Superimposition of Pol λ with the Open and Closed Conformations of Pol βSuperimposition of the α carbon trace of human Pol λ (red) with the structures of human Pol β in an open (1BPX; yellow) and closed (1BPY; blue) conformation. The roman numerals refer to different regions of the Pol λ structure as indicated in the text. The rms deviation was 1.4 Å for 112 C-α atoms for 1BPX and 1.4 Å for 113 C-α atoms for 1BPY.
Figure 7.
Figure 7. Biological Implications of the Pol λ Structure(A) Stereo view of an overlay of the active site of Pol λ with that of Pol β in a closed conformation (1BPY). The DNA corresponds to the Pol λ structure, while the incoming ddCTP (green) and metal ions (gray balls) correspond to Pol β 1BPY. Relevant residues are shown in red (Pol λ) and blue (Pol β). The template strand is gray and the primer terminus is yellow.(B) Electrostatic surface potential of Pol λ and Pol β. The DNA for each of the structures is shown in gray (template) and yellow (primer and downstream primer). The potential ranges from −8 kT/e (red) to 8 kT/e (blue).
The above figures are reprinted by permission from Cell Press: Mol Cell (2004, 13, 561-572) copyright 2004.
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