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2DDG

Crystal structure of uracil-DNA glycosylase in complex with AP:G containing DNA

Summary for 2DDG
Entry DOI10.2210/pdb2ddg/pdb
Related2D3Y
Descriptor5'-D(*AP*TP*GP*TP*TP*GP*CP*(D1P)P*TP*TP*AP*GP*TP*CP*C)-3', 5'-D(*GP*GP*AP*CP*TP*AP*AP*GP*GP*CP*AP*AP*CP*A)-3', uracil-DNA glycosylase, ... (9 entities in total)
Functional Keywordsbase excision repair, uracil-dna glycosylase, iron/sulfer cluster, dna complex, thermophile, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, hydrolase-dna complex, hydrolase/dna
Biological sourceThermus thermophilus
Total number of polymer chains3
Total formula weight34044.92
Authors
Kosaka, H.,Nakagawa, N.,Masui, R.,Hoseki, J.,Kuramitsu, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-01-28, release date: 2007-02-13, Last modification date: 2024-03-13)
Primary citationKosaka, H.,Hoseki, J.,Nakagawa, N.,Kuramitsu, S.,Masui, R.
Crystal structure of family 5 uracil-DNA glycosylase bound to DNA.
J.Mol.Biol., 373:839-850, 2007
Cited by
PubMed Abstract: Uracil-DNA glycosylase (UDG) removes uracil generated by the deamination of cytosine or misincorporation of deoxyuridine monophosphate. Within the UDG superfamily, a fifth UDG family lacks a polar residue in the active-site motif, which mediates the hydrolysis of the glycosidic bond by activation of a water molecule in UDG families 1-4. We have determined the crystal structure of a novel family 5 UDG from Thermus thermophilus HB8 complexed with DNA containing an abasic site. The active-site structure suggests this enzyme uses both steric force and water activation for its excision reaction. A conserved asparagine residue acts as a ligand to the catalytic water molecule. The structure also implies that another water molecule acts as a barrier during substrate recognition. Based on no significant open-closed conformational change upon binding to DNA, we propose a "slide-in" mechanism for initial damage recognition.
PubMed: 17870091
DOI: 10.1016/j.jmb.2007.08.022
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

237735

数据于2025-06-18公开中

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