5c9f
Crystal structure of a retropepsin-like aspartic protease from Rickettsia conoriiCrystal structure of a retropepsin-like aspartic protease from Rickettsia conorii
Structural highlights
Publication Abstract from PubMedThe structure of the decadeoxyribonucleotide d(GCATGCATGC) is presented at a resolution of 1.8 A. The decamer adopts a novel double-folded structure in which the direction of progression of the backbone changes at the two thymine residues. Intra-strand stacking interactions (including an interaction between the endocylic O atom of a ribose moiety and the adjacent purine base), hydrogen bonds and cobalt-ion interactions stabilize the double-folded structure of the single strand. Two such double-folded strands come together in the crystal to form a dimer. Inter-strand Watson-Crick hydrogen bonds form four base pairs. This portion of the decamer structure is similar to that observed in other previously reported oligonucleotide structures and has been dubbed a `bi-loop'. Both the double-folded single-strand structure, as well as the dimeric bi-loop structure, serve as starting points to construct models for triplet-repeat DNA sequences, which have been implicated in many human diseases. The novel double-folded structure of d(GCATGCATGC): a possible model for triplet-repeat sequences.,Thirugnanasambandam A, Karthik S, Mandal PK, Gautham N Acta Crystallogr D Biol Crystallogr. 2015 Oct;71(Pt 10):2119-26. doi:, 10.1107/S1399004715013930. Epub 2015 Sep 30. PMID:26457435[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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