4ix3: Difference between revisions
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==Crystal structure of a Stt7 homolog from Micromonas algae== | ==Crystal structure of a Stt7 homolog from Micromonas algae== | ||
<StructureSection load='4ix3' size='340' side='right' caption='[[4ix3]], [[Resolution|resolution]] 1.35Å' scene=''> | <StructureSection load='4ix3' size='340' side='right'caption='[[4ix3]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ix3]] is a 2 chain structure with sequence from [ | <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"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | </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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/C1EBN1_MICCC C1EBN1_MICCC] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chang | [[Category: Micromonas commoda]] | ||
[[Category: Guo | [[Category: Chang W]] | ||
[[Category: Li | [[Category: Guo J]] | ||
[[Category: Liu | [[Category: Li M]] | ||
[[Category: Pan | [[Category: Liu Z]] | ||
[[Category: Wei | [[Category: Pan X]] | ||
[[Category: Wei X]] | |||
Revision as of 00:16, 17 November 2022
Crystal structure of a Stt7 homolog from Micromonas algaeCrystal structure of a Stt7 homolog from Micromonas algae
Structural highlights
FunctionPublication Abstract from PubMedUnder 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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