6l97

Complex of DNA polymerase IV and L-DNA duplex

spinqualitylabelsall models 6l97, resolution 2.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l97 is a 4 chain structure with sequence from Saccharolobus solfataricus P2 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.362Å Ligands: 0DA, 0DC, 0DG, 0DT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DPO4_SACS2 Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. It is involved in translesional synthesis. Publication Abstract from PubMed The intrinsic l-DNA binding properties of a natural DNA polymerase was discovered. The binding affinity of Dpo4 polymerase for l-DNA was comparable to that for d-DNA. The crystal structure of Dpo4/l-DNA complex revealed a dimer formed by the little finger domain that provides a binding site for l-DNA. The crystal structure of a natural DNA polymerase complexed with mirror DNA.,An J, Choi J, Hwang D, Park J, Pemble CW 4th, Duong THM, Kim KR, Ahn H, Chung HS, Ahn DR Chem Commun (Camb). 2020 Feb 18;56(14):2186-2189. doi: 10.1039/c9cc09351f. Epub, 2020 Jan 23. PMID:31971182 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DNA polymerase 3D structures

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