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5GN3

Structure of selenomethionine-labelled Uracil DNA glycosylase (BdiUNG) from Bradyrhizobium diazoefficiens

Summary for 5GN3
Entry DOI10.2210/pdb5gn3/pdb
Related5GN2 5GNW 5GRK
DescriptorBlr0248 protein (2 entities in total)
Functional Keywordsuracil dna glycosylase (udg), bradyrhizobium diazoefficiens, nitrogen fixing symbiont, hydrolase
Biological sourceBradyrhizobium diazoefficiens USDA 110
Total number of polymer chains4
Total formula weight119841.08
Authors
Patil, V.V.,Chembazhi, U.V.,Varshney, U.,Woo, E. (deposition date: 2016-07-19, release date: 2017-05-03, Last modification date: 2024-11-13)
Primary citationChembazhi, U.V.,Patil, V.V.,Sah, S.,Reeve, W.,Tiwari, R.P.,Woo, E.,Varshney, U.
Uracil DNA glycosylase (UDG) activities in Bradyrhizobium diazoefficiens: characterization of a new class of UDG with broad substrate specificity
Nucleic Acids Res., 45:5863-5876, 2017
Cited by
PubMed Abstract: Repair of uracils in DNA is initiated by uracil DNA glycosylases (UDGs). Family 1 UDGs (Ung) are the most efficient and ubiquitous proteins having an exquisite specificity for uracils in DNA. Ung are characterized by motifs A (GQDPY) and B (HPSPLS) sequences. We report a novel dimeric UDG, Blr0248 (BdiUng) from Bradyrhizobium diazoefficiens. Although BdiUng contains the motif A (GQDPA), it has low sequence identity to known UDGs. BdiUng prefers single stranded DNA and excises uracil, 5-hydroxymethyl-uracil or xanthine from it. BdiUng is impervious to inhibition by AP DNA, and Ugi protein that specifically inhibits family 1 UDGs. Crystal structure of BdiUng shows similarity with the family 4 UDGs in its overall fold but with family 1 UDGs in key active site residues. However, instead of a classical motif B, BdiUng has a uniquely extended protrusion explaining the lack of Ugi inhibition. Structural and mutational analyses of BdiUng have revealed the basis for the accommodation of diverse substrates into its substrate binding pocket. Phylogenetically, BdiUng belongs to a new UDG family. Bradyrhizobium diazoefficiens presents a unique scenario where the presence of at least four families of UDGs may compensate for the absence of an efficient family 1 homologue.
PubMed: 28369586
DOI: 10.1093/nar/gkx209
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.281 Å)
Structure validation

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数据于2025-06-25公开中

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