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5htv

From Proteopedia

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<StructureSection load='5htv' size='340' side='right'caption='[[5htv]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='5htv' size='340' side='right'caption='[[5htv]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5htv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HTV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HTV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5htv]] is a 1 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=5HTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HTV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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]] 1.78&#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]], [[5htx|5htx]], [[5hty|5hty]], [[5hu2|5hu2]], [[5hux|5hux]], [[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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XK-1, At2g21370 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5htv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5htv OCA], [https://pdbe.org/5htv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5htv RCSB], [https://www.ebi.ac.uk/pdbsum/5htv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5htv ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5htv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5htv OCA], [http://pdbe.org/5htv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5htv RCSB], [http://www.ebi.ac.uk/pdbsum/5htv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5htv ProSAT]</span></td></tr>
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</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/XK1_ARATH XK1_ARATH] Exhibits ATP hydrolysis without substrate. Can phosphorylate D-ribulose with low efficiency.<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 5htv" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
 
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[[Category: Large Structures]]
 
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[[Category: Chang, W]]
 
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[[Category: Li, M]]
 
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[[Category: Xie, Y]]
 
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[[Category: Amppnp]]
 
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Putative sugar kinase]]
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[[Category: Large Structures]]
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[[Category: Transferase]]
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[[Category: Chang W]]
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[[Category: Li M]]
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[[Category: Xie Y]]

Current revision

Putative sugar kinases from Arabidopsis thaliana in complex with AMPPNP

PDB ID 5htv

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