2xc9 | pdb_00002xc9

BINARY COMPLEX OF SULFOLOBUS SOLFATARICUS DPO4 DNA POLYMERASE AND 1, N2-ETHENOGUANINE MODIFIED DNA, MAGNESIUM FORM

spinqualitylabelsall models 2xc9, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xc9 is a 3 chain structure with sequence from Sulso. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: GNE Related: 2asl, 1s0m, 2jeg, 1rys, 2v4s, 2j6t, 2w9b, 1n56, 1jx4, 2atl, 2c22, 2va2, 1s97, 2agq, 2jej, 2w9c, 2asj, 2ago, 2w9a, 2asd, 1jxl, 1n48, 2bq3, 2uvu, 2j6u, 2agp, 2c2r, 1s0n, 1s0o, 2jef, 2w8l, 2uvw, 2bqr, 2jei, 1s9f, 2au0, 2bqu, 2c28, 2v9w, 2v4r, 2c2e, 1ryr, 2uvv, 2c2d, 2v4q, 2br0, 1s10, 2j6s, 2uvr, 2va3, 2w8k, 2v4t, 2xca, 2xcp Gene: DPO4 (SULSO) Activity: DNA-directed DNA polymerase, with EC number 2.7.7.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DPO4_SULSO] 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.[HAMAP-Rule:MF_01113] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Crystal structures of a binary Mg2+-form Dpo4-DNA complex with 1,N2-etheno-dG in the template strand as well as of ternary Mg2+-form Dpo4-DNA-dCTP/dGTP complexes with 8-oxoG in the template strand have been determined. Comparison of their conformations and active-site geometries with those of the corresponding Ca2+-form complexes revealed that the DNA and polymerase undergo subtle changes as a result of the catalytically more active Mg2+ occupying both the A and B sites. Metal-ion dependence of the active-site conformation of the translesion DNA polymerase Dpo4 from Sulfolobus solfataricus.,Irimia A, Loukachevitch LV, Eoff RL, Guengerich FP, Egli M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):1013-8. Epub 2010 Aug 21. PMID:20823515 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA