6pbd

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DNA N6-Adenine Methyltransferase CcrM In Complex with Double-Stranded DNA Oligonucleotide Containing Its Recognition Sequence GAATCDNA N6-Adenine Methyltransferase CcrM In Complex with Double-Stranded DNA Oligonucleotide Containing Its Recognition Sequence GAATC

Structural highlights

6pbd is a 4 chain structure with sequence from caulobacter_crescentus_poindexter_1964 Atcc 15252 caulobacter crescentus poindexter 1964. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:ccrMIM, ccrM, CC_0378 (ATCC 15252 Caulobacter crescentus Poindexter 1964)
Activity:Site-specific DNA-methyltransferase (adenine-specific), with EC number 2.1.1.72
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MTC1_CAUVC] This methylase recognizes the double-stranded sequence GANTC and causes specific methylation on A-2 on both strands. Ccrm-mediated methylation has important cellular functions. Appears to contribute to the accurate cell-cycle control of DNA replication and cellular morphology.

Publication Abstract from PubMed

The Caulobacter crescentus cell cycle-regulated DNA methyltransferase (CcrM) methylates the adenine of hemimethylated GANTC after replication. Here we present the structure of CcrM in complex with double-stranded DNA containing the recognition sequence. CcrM contains an N-terminal methyltransferase domain and a C-terminal nonspecific DNA-binding domain. CcrM is a dimer, with each monomer contacting primarily one DNA strand: the methyltransferase domain of one molecule binds the target strand, recognizes the target sequence, and catalyzes methyl transfer, while the C-terminal domain of the second molecule binds the non-target strand. The DNA contacts at the 5-base pair recognition site results in dramatic DNA distortions including bending, unwinding and base flipping. The two DNA strands are pulled apart, creating a bubble comprising four recognized base pairs. The five bases of the target strand are recognized meticulously by stacking contacts, van der Waals interactions and specific Watson-Crick polar hydrogen bonds to ensure high enzymatic specificity.

The cell cycle-regulated DNA adenine methyltransferase CcrM opens a bubble at its DNA recognition site.,Horton JR, Woodcock CB, Opot SB, Reich NO, Zhang X, Cheng X Nat Commun. 2019 Oct 10;10(1):4600. doi: 10.1038/s41467-019-12498-7. PMID:31601797[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Horton JR, Woodcock CB, Opot SB, Reich NO, Zhang X, Cheng X. The cell cycle-regulated DNA adenine methyltransferase CcrM opens a bubble at its DNA recognition site. Nat Commun. 2019 Oct 10;10(1):4600. doi: 10.1038/s41467-019-12498-7. PMID:31601797 doi:http://dx.doi.org/10.1038/s41467-019-12498-7

6pbd, resolution 2.34Å

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