2lj6

Structural highlights

2lj6 is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full experimental information is available from OCA.
Activity: Glucokinase, with EC number 2.7.1.2

Publication Abstract from PubMed

The 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

1. ↑ Natarajan A, Dutta K, Temel DB, Nair PA, Shuman S, Ghose R. Solution structure and DNA-binding properties of the phosphoesterase domain of DNA ligase D. Nucleic Acids Res. 2012 Mar 1;40(5):2076-88. Epub 2011 Nov 13. PMID:22084199 doi:10.1093/nar/gkr950