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A cytosine modification mechanism revealed by the structure of a ternary complex of deoxycytidylate...

A cytosine modification mechanism revealed by the structure of a ternary complex of deoxycytidylate...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_f37ee44c31f14ce3aae92b7601be61ca

A cytosine modification mechanism revealed by the structure of a ternary complex of deoxycytidylate hydroxymethylase from bacteriophage T4 with its cofactor and substrate

About this item

Full title

A cytosine modification mechanism revealed by the structure of a ternary complex of deoxycytidylate hydroxymethylase from bacteriophage T4 with its cofactor and substrate

Publisher

England: International Union of Crystallography

Journal title

IUCrJ, 2019-03, Vol.6 (2), p.206-217

Language

English

Formats

Publication information

Publisher

England: International Union of Crystallography

More information

Scope and Contents

Contents

To protect viral DNA against the host bacterial restriction system, bacteriophages utilize a special modification system – hydroxymethylation – in which dCMP hydroxymethylase (dCH) converts dCMP to 5-hydroxymethyl-dCMP (5hm-dCMP) using
N
5,
N
10-methylenetetrahydrofolate as a cofactor. Despite shared similarity with thymidylate synthase...

Alternative Titles

Full title

A cytosine modification mechanism revealed by the structure of a ternary complex of deoxycytidylate hydroxymethylase from bacteriophage T4 with its cofactor and substrate

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_f37ee44c31f14ce3aae92b7601be61ca

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_f37ee44c31f14ce3aae92b7601be61ca

Other Identifiers

ISSN

2052-2525

E-ISSN

2052-2525

DOI

10.1107/S2052252518018274

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