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Structural insight into the quinolone–DNA cleavage complex of type IIA topoisomerases
- I. Laponogov, M. Sohi, M. Sanderson
- Biology, ChemistryNature Structural &Molecular Biology
- 1 June 2009
The structures of cleavage complexes formed by the Streptococcus pneumoniae ParC breakage-reunion and ParE TOPRIM domains of topoisomerase IV stabilized by moxifloxacin and clinafloxacIn help explain antibacterial quinolone action and resistance.
Structural Basis of Gate-DNA Breakage and Resealing by Type II Topoisomerases
- I. Laponogov, Xiaohui Pan, D. Veselkov, K. McAuley, L. Fisher, M. Sanderson
- Biology, ChemistryPloS one
- 28 June 2010
X-ray crystallography is used to study sequential states in the formation and reversal of a DNA cleavage complex by topoisomerase IV from Streptococcus pneumoniae, the bacterial type II enzyme involved in chromosome segregation to suggest how a type II enzymes reseals DNA during its normal reaction cycle and illuminate aspects of drug arrest important for the development of new topoisomersase-targeting therapeutics.
The SOCS-Box of HIV-1 Vif Interacts with ElonginBC by Induced-Folding to Recruit Its Cul5-Containing Ubiquitin Ligase Complex
It is concluded that HIV-1 Vif engages EloBC via an induced-folding mechanism that does not require additional co-factors, and speculate that these features distinguish Vif from other Elo BC specificity factors such as cellular SOCS proteins, and may enhance the prospects of obtaining therapeutic inhibitors of Vif function.
Cocrystal structure of an editing complex of Klenow fragment with DNA.
- P. Freemont, J. Friedman, L. Beese, M. Sanderson, T. Steitz
- Chemistry, BiologyProceedings of the National Academy of Sciences…
- 1 December 1988
Two divalent metal ions interacting with the phosphodiester to be hydrolyzed are proposed to catalyze the exonuclease reaction by a mechanism that may be related to mechanisms of other enzymes that catalyze phospho-group transfer including RNA enzymes.
Crystal structures of the thymidine kinase from herpes simplex virus type-I in complex with deoxythymidine and Ganciclovir
The crystal structures of thymidine kinase from herpes simplex virus type-1 complexed with its natural substrate deoxythymidine andcomplexed with the guanosine analogue Ganciclovir have been solved and structural similarities provide an insight into the mechanism of nucleoside phosphorylation by thymazine kinase.
Exploring the active site of herpes simplex virus type‐1 thymidine kinase by X‐ray crystallography of complexes with aciclovir and other ligands
The binary complexes of HSV‐1 thymidine kinase (TK) with the drug molecules aciclovir and penciclovIR, determined by X‐ray crystallography at 2.37 Å resolution, are reported for the first time.
Crystal lattice packing is important in determining the bend of a DNA dodecamer containing an adenine tract.
- A. D. DiGabriele, M. Sanderson, T. Steitz
- ChemistryProceedings of the National Academy of Sciences…
- 1 March 1989
The structural features of the static bending of the helical axis exhibited by adenine-tract structures in solution are deduced and it is concluded that the overall bend of 20 degrees in the direction of the major groove observed here arises from the forces associated with crystal packing.
Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I.
Site-directed mutagenesis of the large fragment of DNA polymerase I (Klenow fragment) yielded two mutant proteins lacking 3',5'-exonuclease activity but having normal polymerase activity, which suggest that one metal ion plays a role in substrate binding while the other is involved in catalysis of the exonucleasing reaction.
Structure of an ‘open’ clamp type II topoisomerase-DNA complex provides a mechanism for DNA capture and transport
- I. Laponogov, D. Veselkov, I. Crevel, Xiaohui Pan, L. Fisher, M. Sanderson
- Biology, ChemistryNucleic acids research
- 21 August 2013
The structure shows the molecular conformations of all three gates at 3.7 Å, the highest resolution achieved for the full complex to date, and illuminates the mechanism of DNA capture and transport by a type II topoisomerase.