Structure of nucleoside diphosphate kinase from pacific shrimp (Litopenaeus vannamei) in binary complexes with purine and pyrimidine nucleoside diphosphates. Issue 9 (1st September 2014)
- Record Type:
- Journal Article
- Title:
- Structure of nucleoside diphosphate kinase from pacific shrimp (Litopenaeus vannamei) in binary complexes with purine and pyrimidine nucleoside diphosphates. Issue 9 (1st September 2014)
- Main Title:
- Structure of nucleoside diphosphate kinase from pacific shrimp (Litopenaeus vannamei) in binary complexes with purine and pyrimidine nucleoside diphosphates
- Authors:
- López‐Zavala, Alonso A.
Quintero‐Reyes, Idania E.
Carrasco‐Miranda, Jesús S.
Stojanoff, Vivian
Weichsel, Andrzej
Rudiño‐Piñera, Enrique
Sotelo‐Mundo, Rogerio R. - Abstract:
- <abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Nucleoside diphosphate kinase (NDK; EC 2.7.4.6) is an enzyme that catalyzes the third phosphorylation of nucleoside diphosphates, leading to nucleoside triphosphates for DNA replication. Expression of the NDK from <italic>Litopenaeus vannamei</italic> (<italic>Lv</italic>NDK) is known to be regulated under viral infection. Also, as determined by isothermal titration calorimetry, <italic>Lv</italic>NDK binds both purine and pyrimidine deoxynucleoside diphosphates with high binding affinity for dGDP and dADP and with no heat of binding interaction for dCDP [Quintero‐Reyes <italic>et al.</italic> (2012), <italic>J. Bioenerg. Biomembr.</italic><bold>44</bold>, 325–331]. In order to investigate the differences in selectivity, <italic>Lv</italic>NDK was crystallized as binary complexes with both acceptor (dADP and dCDP) and donor (ADP) phosphate‐group nucleoside diphosphate substrates and their structures were determined. The three structures with purine or pyrimidine nucleotide ligands are all hexameric. Also, the binding of deoxy or ribonucleotides is similar, as in the former a water molecule replaces the hydrogen bond made by Lys11 to the 2′‐hydroxyl group of the ribose moiety. This allows Lys11 to maintain a catalytically favourable conformation independently of the kind of sugar found in the nucleotide. Because of this, shrimp NDK may phosphorylate nucleotide analogues to<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Nucleoside diphosphate kinase (NDK; EC 2.7.4.6) is an enzyme that catalyzes the third phosphorylation of nucleoside diphosphates, leading to nucleoside triphosphates for DNA replication. Expression of the NDK from <italic>Litopenaeus vannamei</italic> (<italic>Lv</italic>NDK) is known to be regulated under viral infection. Also, as determined by isothermal titration calorimetry, <italic>Lv</italic>NDK binds both purine and pyrimidine deoxynucleoside diphosphates with high binding affinity for dGDP and dADP and with no heat of binding interaction for dCDP [Quintero‐Reyes <italic>et al.</italic> (2012), <italic>J. Bioenerg. Biomembr.</italic><bold>44</bold>, 325–331]. In order to investigate the differences in selectivity, <italic>Lv</italic>NDK was crystallized as binary complexes with both acceptor (dADP and dCDP) and donor (ADP) phosphate‐group nucleoside diphosphate substrates and their structures were determined. The three structures with purine or pyrimidine nucleotide ligands are all hexameric. Also, the binding of deoxy or ribonucleotides is similar, as in the former a water molecule replaces the hydrogen bond made by Lys11 to the 2′‐hydroxyl group of the ribose moiety. This allows Lys11 to maintain a catalytically favourable conformation independently of the kind of sugar found in the nucleotide. Because of this, shrimp NDK may phosphorylate nucleotide analogues to inhibit the viral infections that attack this organism.</p> </abstract> … (more)
- Is Part Of:
- Acta crystallographica. Volume 70:Issue 9(2014:Sep.)
- Journal:
- Acta crystallographica
- Issue:
- Volume 70:Issue 9(2014:Sep.)
- Issue Display:
- Volume 70, Issue 9 (2014)
- Year:
- 2014
- Volume:
- 70
- Issue:
- 9
- Issue Sort Value:
- 2014-0070-0009-0000
- Page Start:
- 1150
- Page End:
- 1154
- Publication Date:
- 2014-09-01
- Subjects:
- Crystallography -- Periodicals
Crystals -- Periodicals
548 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)2053-230X ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1107/S2053230X1401557X ↗
- Languages:
- English
- ISSNs:
- 2053-230X
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0612.024200
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- 4338.xml