Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation

Science

Volumn 331, Issue 6020, 2011, Pages 1036-1040

  Song, Jikui ^a   Rechkoblit, Olga ^a   Bestor, Timothy H ^b   Patel, Dinshaw J ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^b Columbia University ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CPG OLIGODEOXYNUCLEOTIDE; DNA; DNA METHYLTRANSFERASE 1;

CHEMICAL BINDING; ENZYME ACTIVITY; INHIBITION; RODENT;

ARTICLE; COMPLEX FORMATION; DNA METHYLATION; DNA STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GENE INSERTION; GENE MUTATION; GENETIC STABILITY; HUMAN; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DINUCLEOSIDE PHOSPHATES; DNA; DNA (CYTOSINE-5-)-METHYLTRANSFERASE; DNA METHYLATION; DNA-CYTOSINE METHYLASES; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 79952053850     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1195380     Document Type: Article

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20. The research was supported by funds from the Abby Rockefeller Mauze Trust and Maloris Foundation to D.J.P. and from NIH to T.H.B. We thank S. Murakami for technical assistance and Z. Wang and H. Li for their assistance with x-ray data collection and structure determination. We would also like to thank the staff of NE-CAT beamlines at the Advanced Photon Source, Argonne National Laboratory, and the X-29 beamline at the Brookhaven National Laboratory, for access and assistance with data collection. The structures of the complexes have been deposited in the Protein Data Bank (PDB). The accession codes are mDNMT1(650-1602)-DNA complex with bound AdoHcy (3PT6), hDNMT1(646-1600)-DNA complex with bound AdoHcy (3PTA) and mDNMT1(731-1602) with bound AdoHcy (3PT9).