Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5MVQ

Crystal structure of an unmodified, self-complementary dodecamer.

Summary for 5MVQ
Entry DOI10.2210/pdb5mvq/pdb
DescriptorDNA, MAGNESIUM ION (3 entities in total)
Functional Keywordsa-dna, unmodified, self-complementary, dna
Biological sourcesynthetic construct
Total number of polymer chains2
Total formula weight7375.39
Authors
Hardwick, J.S.,Ptchelkine, D.,Phillips, S.E.V.,Brown, T. (deposition date: 2017-01-17, release date: 2017-05-10, Last modification date: 2024-01-17)
Primary citationHardwick, J.S.,Ptchelkine, D.,El-Sagheer, A.H.,Tear, I.,Singleton, D.,Phillips, S.E.V.,Lane, A.N.,Brown, T.
5-Formylcytosine does not change the global structure of DNA.
Nat. Struct. Mol. Biol., 24:544-552, 2017
Cited by
PubMed Abstract: The mechanism by which the recently identified DNA modification 5-formylcytosine (C) is recognized by epigenetic writer and reader proteins is not known. Recently, an unusual DNA structure, F-DNA, has been proposed as the basis for enzyme recognition of clusters of C. We used NMR and X-ray crystallography to compare several modified DNA duplexes with unmodified analogs and found that in the crystal state the duplexes all belong to the A family, whereas in solution they are all members of the B family. We found that, contrary to previous findings, C does not significantly affect the structure of DNA, although there are modest local differences at the modification sites. Hence, global conformation changes are unlikely to account for the recognition of this modified base, and our structural data favor a mechanism that operates at base-pair resolution for the recognition of C by epigenome-modifying enzymes.
PubMed: 28504696
DOI: 10.1038/nsmb.3411
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.604 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon