Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases (Q27641295)

1

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Olof Bjornberg

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Per Olof Nyman

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Sine Larsen

Journal of Biological Chemistry

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language of work or name

English

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publication date

25 July 2003

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published in

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volume

278

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page(s)

27916-22

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issue

30

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cites work

A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii

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The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase

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Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli

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Pseudouridine synthases: four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases

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Protein sequence comparisons show that the 'pseudoproteases' encoded by poxviruses and certain retroviruses belong to the deoxyuridine triphosphatase family

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Crystal structure of a dUTPase

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Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex

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The crystallography beamline I711 at MAX II.

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Reciprocal-space solvent flattening

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Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target

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Identifiers

DOI

10.1074/JBC.M304361200

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Consolidated OpenCitations Corpus – April 2017

2392518

2392518

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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