Back to Search
Start Over
Crystal Structures of Putative Sugar Kinases from Synechococcus Elongatus PCC 7942 and Arabidopsis Thaliana
- Source :
- PLoS ONE, Vol 11, Iss 5, p e0156067 (2016), PLoS ONE
- Publication Year :
- 2016
- Publisher :
- Public Library of Science (PLoS), 2016.
-
Abstract
- The genome of the Synechococcus elongatus strain PCC 7942 encodes a putative sugar kinase (SePSK), which shares 44.9% sequence identity with the xylulose kinase-1 (AtXK-1) from Arabidopsis thaliana. Sequence alignment suggests that both kinases belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases. However, their exact physiological function and real substrates remain unknown. Here we solved the structures of SePSK and AtXK-1 in both their apo forms and in complex with nucleotide substrates. The two kinases exhibit nearly identical overall architecture, with both kinases possessing ATP hydrolysis activity in the absence of substrates. In addition, our enzymatic assays suggested that SePSK has the capability to phosphorylate D-ribulose. In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK. Using mutation and activity analysis, we further verified the key residues important for its catalytic activity. Moreover, our structural comparison with other family members suggests that there are major conformational changes in SePSK upon substrate binding, facilitating the catalytic process. Together, these results provide important information for a more detailed understanding of the cofactor and substrate binding mode as well as the catalytic mechanism of SePSK, and possible similarities with its plant homologue AtXK-1.
- Subjects :
- 0301 basic medicine
Glycerol
Arabidopsis
lcsh:Medicine
Crystallography, X-Ray
Biochemistry
ATP hydrolysis
Chemical reactions
Catalytic Domain
Transferase
Arabidopsis thaliana
lcsh:Science
Synechococcus
Multidisciplinary
Crystallography
biology
Kinase
Organic Compounds
Hydrolysis
Physics
Condensed Matter Physics
Enzyme structure
Chemistry
Phosphotransferases (Alcohol Group Acceptor)
Bioassays and Physiological Analysis
Physical Sciences
Crystal Structure
Phosphorylation
Research Article
Materials by Structure
Materials Science
Pentoses
Carbohydrates
Sequence alignment
Monomers (Chemistry)
Research and Analysis Methods
Crystals
03 medical and health sciences
Bacterial Proteins
Electron Density
Solid State Physics
Polymer chemistry
Enzyme Assays
Arabidopsis Proteins
Organic Chemistry
lcsh:R
Chemical Compounds
Biology and Life Sciences
biology.organism_classification
030104 developmental biology
Enzyme Structure
Enzymology
lcsh:Q
Biochemical Analysis
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 11
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....a4e58ca07eff41e4ab7a92d9f35e55cb