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| | ==Crystal structure of shikimate kinase from Arabidopsis thaliana (AtSK2)== | | ==Crystal structure of shikimate kinase from Arabidopsis thaliana (AtSK2)== |
| - | <StructureSection load='3nwj' size='340' side='right' caption='[[3nwj]], [[Resolution|resolution]] 2.35Å' scene=''> | + | <StructureSection load='3nwj' size='340' side='right'caption='[[3nwj]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nwj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NWJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NWJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nwj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NWJ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At4g39540, At4g39540/F23K16_170 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nwj OCA], [https://pdbe.org/3nwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nwj RCSB], [https://www.ebi.ac.uk/pdbsum/3nwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nwj ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nwj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nwj RCSB], [http://www.ebi.ac.uk/pdbsum/3nwj PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SK2_ARATH SK2_ARATH] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.<ref>PMID:19057671</ref> <ref>PMID:21520319</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3nwj" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Shikimate kinase|Shikimate kinase]] | + | *[[Shikimate kinase 3D structures|Shikimate kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Arabidopsis thaliana]] | | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Shikimate kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Christendat, D]] | + | [[Category: Christendat D]] |
| - | [[Category: Fucile, G]] | + | [[Category: Fucile G]] |
| - | [[Category: Garcia, C]] | + | [[Category: Garcia C]] |
| - | [[Category: Petit, P]] | + | [[Category: Petit P]] |
| - | [[Category: Atp binding]]
| + | |
| - | [[Category: Chloroplast]]
| + | |
| - | [[Category: Nucleoside monophosphate kinase]]
| + | |
| - | [[Category: P loop]]
| + | |
| - | [[Category: Shikimate]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
SK2_ARATH Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.[1] [2]
Publication Abstract from PubMed
The expression of plant shikimate kinase (SK; EC 2.7.1.71), an intermediate step in the shikimate pathway to aromatic amino acid biosynthesis, is induced under specific conditions of environmental stress and developmental requirements in an isoform-specific manner. Despite their important physiological role, experimental structures of plant SKs have not been determined and the biochemical nature of plant SK regulation is unknown. The Arabidopsis thaliana genome encodes two SKs, AtSK1 and AtSK2. We demonstrate that AtSK2 is highly unstable and becomes inactivated at 37 degrees C whereas the heat-induced isoform, AtSK1, is thermostable and fully active under identical conditions at this temperature. We determined the crystal structure of AtSK2, the first SK structure from the plant kingdom, and conducted biophysical characterizations of both AtSK1 and AtSK2 towards understanding this mechanism of thermal regulation. The crystal structure of AtSK2 is generally conserved with bacterial SKs with the addition of a putative regulatory phosphorylation motif forming part of the adenosine triphosphate binding site. The heat-induced isoform, AtSK1, forms a homodimer in solution, the formation of which facilitates its relative thermostability compared to AtSK2. In silico analyses identified AtSK1 site variants that may contribute to AtSK1 stability. Our findings suggest that AtSK1 performs a unique function under heat stress conditions where AtSK2 could become inactivated. We discuss these findings in the context of regulating metabolic flux to competing downstream pathways through SK-mediated control of steady state concentrations of shikimate.
Structural and biochemical investigation of two Arabidopsis shikimate kinases: The heat-inducible isoform is thermostable.,Fucile G, Garcia C, Carlsson J, Sunnerhagen M, Christendat D Protein Sci. 2011 Jul;20(7):1125-36. doi: 10.1002/pro.640. Epub 2011 May, 31. PMID:21520319[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fucile G, Falconer S, Christendat D. Evolutionary diversification of plant shikimate kinase gene duplicates. PLoS Genet. 2008 Dec;4(12):e1000292. doi: 10.1371/journal.pgen.1000292. Epub 2008, Dec 5. PMID:19057671 doi:10.1371/journal.pgen.1000292
- ↑ Fucile G, Garcia C, Carlsson J, Sunnerhagen M, Christendat D. Structural and biochemical investigation of two Arabidopsis shikimate kinases: The heat-inducible isoform is thermostable. Protein Sci. 2011 Jul;20(7):1125-36. doi: 10.1002/pro.640. Epub 2011 May, 31. PMID:21520319 doi:10.1002/pro.640
- ↑ Fucile G, Garcia C, Carlsson J, Sunnerhagen M, Christendat D. Structural and biochemical investigation of two Arabidopsis shikimate kinases: The heat-inducible isoform is thermostable. Protein Sci. 2011 Jul;20(7):1125-36. doi: 10.1002/pro.640. Epub 2011 May, 31. PMID:21520319 doi:10.1002/pro.640
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