2c49: Difference between revisions

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[[Category: transferase]]
[[Category: transferase]]


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Revision as of 17:52, 30 October 2007

File:2c49.gif


2c49, resolution 1.92Å

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CRYSTAL STRUCTURE OF METHANOCALDOCOCCUS JANNASCHII NUCLEOSIDE KINASE- AN ARCHAEAL MEMBER OF THE RIBOKINASE FAMILY

OverviewOverview

Nucleoside kinase from the hyperthermophilic archaeon Methanocaldococcus, jannaschii (MjNK) is a member of the ribokinase family. In the presence of, ATP and Mg(2+), MjNK is able to catalyze the phosphorylation of a variety, of nucleosides, including inosine, cytidine, guanosine and adenosine., Here, the crystal structure of MjNK, the first structure of an archaeal, representative of the ribokinase family, is presented. The structure was, solved using the multiple-wavelength anomalous dispersion technique., Three-dimensional structures of the unliganded enzyme and a complex of, MjNK, an ATP analogue and adenosine were determined to 1.7 and 1.9 A, resolution, respectively. Each subunit comprises an alpha/beta-domain and, a smaller lid domain and has an overall fold characteristic of the, ... [(full description)]

About this StructureAbout this Structure

2C49 is a [Single protein] structure of sequence from [Methanocaldococcus jannaschii] with MG, ADN and ANP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Structure of Methanocaldococcus jannaschii nucleoside kinase: an archaeal member of the ribokinase family., Arnfors L, Hansen T, Schonheit P, Ladenstein R, Meining W, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1085-97. Epub 2006, Aug 19. PMID:16929110

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OCA