4ix3: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4ix3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonas_commoda Micromonas commoda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IX3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 1.35&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4ix3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ix3 OCA], [https://pdbe.org/4ix3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ix3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ix3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ix3 ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/C1EBN1_MICCC C1EBN1_MICCC]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Under natural environments, plants and algae have evolved various photosynthetic acclimation mechanisms in response to the constantly changing light conditions. The state transition and long-term response processes in photosynthetic acclimation involve remodeling and composition alteration of thylakoid membrane. A chloroplast protein kinase named Stt7/STN7 has been found to have pivotal roles in both state transition and long-term response. Here we report the crystal structures of the kinase domain of a putative Stt7/STN7 homolog from Micromonas sp. RCC299 (MsStt7d) in the apo form and in complex with various nucleotide substrates. MsStt7d adopts a canonical protein kinase fold and contains all the essential residues at the active site. A novel hairpin motif, found to be a conserved feature of the Stt7/STN7 family and indispensable for the kinase stability, interacts with the activation loop and fixes it in an active conformation. We have also demonstrated that MsStt7d is a dualspecifi city kinase that phosphorylates both Thr and Tyr residues. Moreover, preliminary in vitro data suggest that it might be capable of phosphorylating a consensus N-terminal pentapeptide of light-harvesting proteins Micromonas Lhcp4 and Arabidopsis Lhcb1 directly. The potential peptide/protein substrate binding site is predicted based on the location of a pseudo-substrate contributed by the adjacent molecule within the crystallographic dimer. The structural and biochemical data presented here provide a framework for an improved understanding on the role of Stt7/STN7 in photosynthetic acclimation.
-Structure of the catalytic domain of a state transition kinase homolog from Micromonas algae.,Guo J, Wei X, Li M, Pan X, Chang W, Liu Z Protein Cell. 2013 Aug;4(8):607-19. doi: 10.1007/s13238-013-3034-9. Epub 2013 Jun, 23. PMID:23794031<ref>PMID:23794031</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ix3" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>