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Structure-function analysis of a bacterial deoxyadenosine kinase reveals the basis for substrate specificity.

Abstract：

:Deoxyribonucleoside kinases (dNKs) catalyze the transfer of a phosphoryl group from ATP to a deoxyribonucleoside (dN), a key step in DNA precursor synthesis. Recently structural information concerning dNKs has been obtained, but no structure of a bacterial dCK/dGK enzyme is known. Here we report the structure of such an enzyme, represented by deoxyadenosine kinase from Mycoplasma mycoides subsp. mycoides small colony type (Mm-dAK). Superposition of Mm-dAK with its human counterpart's deoxyguanosine kinase (dGK) and deoxycytidine kinase (dCK) reveals that the overall structures are very similar with a few amino acid alterations in the proximity of the active site. To investigate the substrate specificity, Mm-dAK has been crystallized in complex with dATP and dCTP, as well as the products dCMP and dCDP. Both dATP and dCTP bind to the enzyme in a feedback-inhibitory manner with the dN part in the deoxyribonucleoside binding site and the triphosphates in the P-loop. Substrate specificity studies with clinically important nucleoside analogs as well as several phosphate donors were performed. Thus, in this study we combine structural and kinetic data to gain a better understanding of the substrate specificity of the dCK/dGK family of enzymes. The structure of Mm-dAK provides a starting point for making new anti bacterial agents against pathogenic bacteria.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Welin M,Wang L,Eriksson S,Eklund H

doi

10.1016/j.jmb.2006.12.010

subject

Has Abstract

pub_date

2007-03-09 00:00:00

pages

1615-23

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(06)01669-X

journal_volume

366

pub_type

杂志文章

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