Structural highlights2lj6 is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full experimental information is available from OCA. Publication Abstract from PubMedThe phosphoesterase (PE) domain of the bacterial DNA repair enzyme LigD possesses distinctive manganese-dependent 3'-phosphomonoesterase and 3'-phosphodiesterase activities. PE exemplifies a new family of DNA end-healing enzymes found in all phylogenetic domains. Here, we determined the structure of the PE domain of Pseudomonas aeruginosa LigD (PaePE) using solution NMR methodology. PaePE has a disordered N-terminus and a well-folded core that differs in instructive ways from the crystal structure of a PaePE*Mn(2+)* sulfate complex, especially at the active site that is found to be conformationally dynamic. Chemical shift perturbations in the presence of primer-template duplexes with 3'-deoxynucleotide, 3'-deoxynucleotide 3'-phosphate, or 3' ribonucleotide termini reveal the surface used by PaePE to bind substrate DNA and suggest a more efficient engagement in the presence of a 3'-ribonucleotide. Spectral perturbations measured in the presence of weakly catalytic (Cd(2+)) and inhibitory (Zn(2+)) metals provide evidence for significant conformational changes at and near the active site, compared to the relatively modest changes elicited by Mn(2+). Solution structure and DNA-binding properties of the phosphoesterase domain of DNA ligase D.,Natarajan A, Dutta K, Temel DB, Nair PA, Shuman S, Ghose R Nucleic Acids Res. 2012 Mar 1;40(5):2076-88. Epub 2011 Nov 13. PMID:22084199[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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