(Q27641504)

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Crystal complexes of a predicted S-adenosylmethionine-dependent methyltransferase reveal a typical AdoMet binding domain and a substrate recognition domain

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scholarly article

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Crystal complexes of a predicted S-adenosylmethionine-dependent methyltransferase reveal a typical AdoMet binding domain and a substrate recognition domain (English)

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Elena Evdokimova

3

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Alexei Savchenko

4

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5

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Wayne F. Anderson

6

object named as

Wayne F Anderson

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author name string

Darcie J Miller

1

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Nancy Ouellette

2

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publication date

July 2003

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Protein Science

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12

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7

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1432-42

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Structure of a binary complex of HhaI methyltransferase with S-adenosyl-L-methionine formed in the presence of a short non-specific DNA oligonucleotide

1 reference

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DNA containing 4'-thio-2'-deoxycytidine inhibits methylation by HhaI methyltransferase

1 reference

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Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine

1 reference

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HhaI methyltransferase flips its target base out of the DNA helix

1 reference

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1 reference

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1 reference

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1 reference

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Multiple sequence alignment with Clustal X

1 reference

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7 April 2017

SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold

1 reference

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1 reference

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Lack of S-adenosylmethionine results in a cell division defect in Escherichia coli

1 reference

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29 September 2017

Structure and function of DNA methyltransferases.

1 reference

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29 September 2017

mraW, an essential gene at the dcw cluster of Escherichia coli codes for a cytoplasmic protein with methyltransferase activity

1 reference

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Direct phase determination based on anomalous scattering.

1 reference

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2 June 2018

Comparison of protein structures reveals monophyletic origin of the AdoMet-dependent methyltransferase family and mechanistic convergence rather than recent differentiation of N4-cytosine and N6-adenine DNA methylation

1 reference

https://pubmed.ncbi.nlm.nih.gov/12824489

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Processing of X-ray diffraction data collected in oscillation mode

1 reference

https://pubmed.ncbi.nlm.nih.gov/12824489

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1110/PS.0302403

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