6B1R
Hydrogen Bonding Complementary, not size complementarity is key in the formation of the double helix
Summary for 6B1R
Entry DOI | 10.2210/pdb6b1r/pdb |
Descriptor | Reverse transcriptase, DNA (5'-D(*CP*TP*TP*AP*TP*(1WA)P*(1WA)P*(1WA))-3'), DNA (5'-D(P*(IGU)P*(IGU)P*(IGU)P*AP*TP*AP*AP*G)-3'), ... (4 entities in total) |
Functional Keywords | protein-dna, aegis, unnatural base pair, host-guest system, dna binding protein, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Moloney murine leukemia virus (MoMLV) More |
Total number of polymer chains | 3 |
Total formula weight | 34327.11 |
Authors | Singh, I.,Georgiadis, M.M. (deposition date: 2017-09-18, release date: 2018-09-19, Last modification date: 2023-10-04) |
Primary citation | Hoshika, S.,Singh, I.,Switzer, C.,Molt Jr., R.W.,Leal, N.A.,Kim, M.J.,Kim, M.S.,Kim, H.J.,Georgiadis, M.M.,Benner, S.A. "Skinny" and "Fat" DNA: Two New Double Helices. J. Am. Chem. Soc., 140:11655-11660, 2018 Cited by PubMed Abstract: According to the iconic model, the Watson-Crick double helix exploits nucleobase pairs that are both size complementary (big purines pair with small pyrimidines) and hydrogen bond complementary (hydrogen bond donors pair with hydrogen bond acceptors). Using a synthetic biology strategy, we report here the discovery of two new DNA-like systems that appear to support molecular recognition with the same proficiency as standard Watson-Crick DNA. However, these both violate size complementarity (big pairs with small), retaining hydrogen bond complementarity (donors pair with acceptors) as their only specificity principle. They exclude mismatches as well as standard Watson-Crick DNA excludes mismatches. In crystal structures, these "skinny" and "fat" systems form the expected hydrogen bonds, while conferring novel minor groove properties to the resultant duplex regions of the DNA oligonucleotides. Further, computational tools, previously tested primarily on natural DNA, appear to work well for these two new molecular recognition systems, offering a validation of the power of modern computational biology. These new molecular recognition systems may have application in materials science and synthetic biology, and in developing our understanding of alternative ways that genetic information might be stored and transmitted. PubMed: 30148365DOI: 10.1021/jacs.8b05042 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
Download full validation report