2c7p
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HHAI DNA METHYLTRANSFERASE COMPLEX WITH OLIGONUCLEOTIDE CONTAINING 2-AMINOPURINE OPPOSITE TO THE TARGET BASE (GCGC:GMPC) AND SAH
OverviewOverview
DNA base flipping is an important mechanism in molecular enzymology, but, its study is limited by the lack of an accessible and reliable diagnostic, technique. A series of crystalline complexes of a DNA methyltransferase, M.HhaI, and its cognate DNA, in which a fluorescent nucleobase analogue, 2-aminopurine (AP), occupies defined positions with respect the target, flipped base, have been prepared and their structures determined at higher, than 2 A resolution. From time-resolved fluorescence measurements of these, single crystals, we have established that the fluorescence decay function, of AP shows a pronounced, characteristic response to base flipping: the, loss of the very short (approximately 100 ps) decay component and the, large increase in the amplitude of the long (approximately 10 ... [(full description)]
About this StructureAbout this Structure
2C7P is a [Protein complex] structure of sequences from [Haemophilus haemolyticus] with SO4, SAH, EPE and CIT as [ligands]. Active as [DNA (cytosine-5-)-methyltransferase], with EC number [2.1.1.37]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Time-resolved fluorescence of 2-aminopurine as a probe of base flipping in M.HhaI-DNA complexes., Neely RK, Daujotyte D, Grazulis S, Magennis SW, Dryden DT, Klimasauskas S, Jones AC, Nucleic Acids Res. 2005 Dec 9;33(22):6953-60. Print 2005. PMID:16340006
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