5hux

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==Putative sugar kinases from Synechococcus elongatus PCC7942 in complex with ADP==
==Putative sugar kinases from Synechococcus elongatus PCC7942 in complex with ADP==
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<StructureSection load='5hux' size='340' side='right' caption='[[5hux]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
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<StructureSection load='5hux' size='340' side='right'caption='[[5hux]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hux]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HUX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HUX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5htn|5htn]], [[5htj|5htj]], [[5htp|5htp]], [[5htr|5htr]], [[5htv|5htv]], [[5htx|5htx]], [[5hty|5hty]], [[5hu2|5hu2]], [[5hv7|5hv7]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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<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=5hux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hux OCA], [http://pdbe.org/5hux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hux RCSB], [http://www.ebi.ac.uk/pdbsum/5hux PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hux OCA], [https://pdbe.org/5hux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hux RCSB], [https://www.ebi.ac.uk/pdbsum/5hux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hux ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/PSK_SYNE7 PSK_SYNE7] Exhibits ATP hydrolysis without substrate. Phosphorylates D-ribulose.<ref>PMID:27223615</ref>
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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.
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Crystal Structures of Putative Sugar Kinases from Synechococcus Elongatus PCC 7942 and Arabidopsis Thaliana.,Xie Y, Li M, Chang W PLoS One. 2016 May 25;11(5):e0156067. doi: 10.1371/journal.pone.0156067., eCollection 2016. PMID:27223615<ref>PMID:27223615</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5hux" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chang, W]]
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[[Category: Large Structures]]
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[[Category: Li, M]]
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[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
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[[Category: Xie, Y]]
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[[Category: Chang W]]
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[[Category: Adp]]
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[[Category: Li M]]
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[[Category: Complex]]
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[[Category: Xie Y]]
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[[Category: Putative sugar kinase]]
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[[Category: Synechococcus elongatus pcc7942]]
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[[Category: Transferase]]
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Current revision

Putative sugar kinases from Synechococcus elongatus PCC7942 in complex with ADP

PDB ID 5hux

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