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==Crystal structure of a Stt7 homolog from Micromonas algae in complex with AMP-PNP== | |||
<StructureSection load='4ix5' size='340' side='right' caption='[[4ix5]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ix5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Micromonas_sp._rcc299 Micromonas sp. rcc299]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IX5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IX5 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ix3|4ix3]], [[4ix4|4ix4]], [[4ix6|4ix6]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STT7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=296587 Micromonas sp. RCC299])</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=4ix5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ix5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ix5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ix5 PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Micromonas sp. rcc299]] | [[Category: Micromonas sp. rcc299]] | ||
[[Category: Chang, W | [[Category: Chang, W]] | ||
[[Category: Guo, J | [[Category: Guo, J]] | ||
[[Category: Li, M | [[Category: Li, M]] | ||
[[Category: Liu, Z | [[Category: Liu, Z]] | ||
[[Category: Pan, X | [[Category: Pan, X]] | ||
[[Category: Wei, X | [[Category: Wei, X]] | ||
[[Category: Atp binding]] | [[Category: Atp binding]] | ||
[[Category: Canonical protein kinase fold]] | [[Category: Canonical protein kinase fold]] | ||
[[Category: Protein kinase]] | [[Category: Protein kinase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 16:00, 21 December 2014
Crystal structure of a Stt7 homolog from Micromonas algae in complex with AMP-PNPCrystal structure of a Stt7 homolog from Micromonas algae in complex with AMP-PNP
Structural highlights
Publication 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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