3CR8
Hexameric APS kinase from Thiobacillus denitrificans
Summary for 3CR8
Entry DOI | 10.2210/pdb3cr8/pdb |
Descriptor | Sulfate adenylyltransferase, adenylylsulfate kinase (2 entities in total) |
Functional Keywords | aps kinase, adenylylsulfate kinase, transferase, sulfate metabolism, nucleotide 2 kinase, nucleotidyltransferase |
Biological source | Thiobacillus denitrificans (strain ATCC 25259) |
Total number of polymer chains | 3 |
Total formula weight | 184914.96 |
Authors | Gay, S.C.,Segel, I.H.,Fisher, A.J. (deposition date: 2008-04-04, release date: 2009-02-17, Last modification date: 2023-08-30) |
Primary citation | Gay, S.C.,Segel, I.H.,Fisher, A.J. Structure of the two-domain hexameric APS kinase from Thiobacillus denitrificans: structural basis for the absence of ATP sulfurylase activity. Acta Crystallogr.,Sect.D, 65:1021-1031, 2009 Cited by PubMed Abstract: The Tbd_0210 gene of the chemolithotrophic bacterium Thiobacillus denitrificans is annotated to encode a 60.5 kDa bifunctional enzyme with ATP sulfurylase and APS kinase activity. This putative bifunctional enzyme was cloned, expressed and structurally characterized. The 2.95 A resolution X-ray crystal structure reported here revealed a hexameric assembly with D(3) symmetry. Each subunit contains a large N-terminal sulfurylase-like domain and a C-terminal APS kinase domain reminiscent of the two-domain fungal ATP sulfurylases of Penicillium chrysogenum and Saccharomyces cerevisiae, which also exhibit a hexameric assembly. However, the T. denitrificans enzyme exhibits numerous structural and sequence differences in the N-terminal domain that render it inactive with respect to ATP sulfurylase activity. Surprisingly, the C-terminal domain does indeed display APS kinase activity, indicating that this gene product is a true APS kinase. Therefore, these results provide the first structural insights into a unique hexameric APS kinase that contains a nonfunctional ATP sulfurylase-like domain of unknown function. PubMed: 19770499DOI: 10.1107/S0907444909026547 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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