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2KIF

Solution NMR structure of an O6-methylguanine DNA methyltransferase family protein from Vibrio parahaemolyticus. Northeast Structural Genomics Consortium target VpR247.

Summary for 2KIF
Entry DOI10.2210/pdb2kif/pdb
NMR InformationBMRB: 16272
DescriptorO6-methylguanine-DNA methyltransferase (1 entity in total)
Functional Keywordsmethods development, solution nmr structure, dna base repair, o6 methylguanine methyltransferase, nesg, psi-2, methyltransferase, transferase, structural genomics, protein structure initiative, northeast structural genomics consortium
Biological sourceVibrio parahaemolyticus AQ3810
Total number of polymer chains1
Total formula weight12341.31
Authors
Primary citationAramini, J.M.,Tubbs, J.L.,Kanugula, S.,Rossi, P.,Ertekin, A.,Maglaqui, M.,Hamilton, K.,Ciccosanti, C.T.,Jiang, M.,Xiao, R.,Soong, T.T.,Rost, B.,Acton, T.B.,Everett, J.K.,Pegg, A.E.,Tainer, J.A.,Montelione, G.T.
Structural basis of O6-alkylguanine recognition by a bacterial alkyltransferase-like DNA repair protein.
J.Biol.Chem., 285:13736-13741, 2010
Cited by
PubMed Abstract: Alkyltransferase-like proteins (ATLs) are a novel class of DNA repair proteins related to O(6)-alkylguanine-DNA alkyltransferases (AGTs) that tightly bind alkylated DNA and shunt the damaged DNA into the nucleotide excision repair pathway. Here, we present the first structure of a bacterial ATL, from Vibrio parahaemolyticus (vpAtl). We demonstrate that vpAtl adopts an AGT-like fold and that the protein is capable of tightly binding to O(6)-methylguanine-containing DNA and disrupting its repair by human AGT, a hallmark of ATLs. Mutation of highly conserved residues Tyr(23) and Arg(37) demonstrate their critical roles in a conserved mechanism of ATL binding to alkylated DNA. NMR relaxation data reveal a role for conformational plasticity in the guanine-lesion recognition cavity. Our results provide further evidence for the conserved role of ATLs in this primordial mechanism of DNA repair.
PubMed: 20212037
DOI: 10.1074/jbc.M109.093591
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227561

数据于2024-11-20公开中

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