Literature DB >> 15299754

Crystallization and preliminary X-ray analysis of bacteriophage T4 deoxynucleotide kinase.

P Sebastiao1, G Obmolova, G S Brush, M J Bessman, A Teplyakov.   

Abstract

T4 deoxynucleotide kinase catalyzes the phosphorylation of 5-hydroxymethyldeoxycytidylate, dTMP and dGMP while excluding dCMP and dAMP. In order to understand the mechanism of this remarkable specificity, the enzyme was over-expressed in Escherichia coli, purified and crystallized for X-ray diffraction analysis. The crystals belong to the monoclinic space group C2 with cell dimensions a = 155.2, b = 58.5, c = 75.7 A, beta = 108.1 degrees. There are two protein monomers in the asymmetric unit related by a twofold axis. Diffraction data to 2.0 A resolution have been collected.

Entities:  

Year:  1996        PMID: 15299754     DOI: 10.1107/S0907444995007281

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Crystal structure of bacteriophage T4 deoxynucleotide kinase with its substrates dGMP and ATP.

Authors:  A Teplyakov; P Sebastiao; G Obmolova; A Perrakis; G S Brush; M J Bessman; K S Wilson
Journal:  EMBO J       Date:  1996-07-15       Impact factor: 11.598

  1 in total

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