8tg0
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8tg0 is ON HOLD Authors: Pougy, K.C., Almeida, F.C.L., Pinheiro, A.S. Description: AtGRP2-CSD Category: Unreleased Structures [[Category: Pougy...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution NMR structure of the cold shock domain of the Arabidopsis thaliana glycine-rich protein AtGRP2== | |
| + | <StructureSection load='8tg0' size='340' side='right'caption='[[8tg0]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8tg0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TG0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=8tg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tg0 OCA], [https://pdbe.org/8tg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tg0 RCSB], [https://www.ebi.ac.uk/pdbsum/8tg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tg0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CSP2_ARATH CSP2_ARATH] Chaperone that binds to RNA, single- (ssDNA) and double-stranded (dsDNA) DNA, and unwinds nucleic acid duplex. Accelerates seed germination and seedling growth under cold stress, and contributes to enhancement of cold and freezing tolerance. Regulates flowering transition, and flower and seed development. Promotes seed germination under salt stress. May regulate respiratory oxygen uptake.<ref>PMID:17123099</ref> <ref>PMID:17169986</ref> <ref>PMID:17376161</ref> <ref>PMID:17963727</ref> <ref>PMID:19258348</ref> <ref>PMID:19269998</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | AtGRP2 is a glycine-rich, RNA-binding protein that plays pivotal roles in abiotic stress response and flowering time regulation in Arabidopsis thaliana. AtGRP2 consists of an N-terminal cold shock domain (CSD) and two C-terminal CCHC-type zinc knuckles interspersed with glycine-rich regions. Here, we investigated the structure, dynamics, and nucleic acid binding properties of AtGRP2-CSD. The 2D [(1)H,(15)N] HSQC spectrum of AtGRP2-CSD(1-79) revealed the presence of a partially folded intermediate in equilibrium with the folded state. The addition of eleven residues at the C-terminus stabilized the folded conformation. The three-dimensional structure of AtGRP2-CSD(1-90) unveiled a beta-barrel composed of five antiparallel beta-strands and a 3(10) helical turn, along with an ordered C-terminal extension, a conserved feature in eukaryotic CSDs. Direct contacts between the C-terminal extension and the beta3-beta4 loop further stabilized the CSD fold. AtGRP2-CSD(1-90) exhibited nucleic acid binding via solvent-exposed residues on strands beta2 and beta3, as well as the beta3-beta4 loop, with higher affinity for DNA over RNA, particularly favoring pyrimidine-rich sequences. Furthermore, DNA binding induced rigidity in the beta3-beta4 loop, evidenced by (15)N-(1)H NOE values. Mutation of residues W17, F26, and F37, in the central beta-sheet, completely abolished DNA binding, highlighting the significance of pi-stacking interactions in the binding mechanism. These results shed light on the mechanism of nucleic acid recognition employed by AtGRP2, creating a framework for the development of biotechnological strategies aimed at enhancing plant resistance to abiotic stresses. | ||
| - | + | Structural basis of nucleic acid recognition by the N-terminal cold shock domain of the plant glycine-rich protein AtGRP2.,Pougy KC, Moraes BS, Malizia-Motta CLF, Lima LMTR, Sachetto-Martins G, Almeida FCL, Pinheiro AS J Biol Chem. 2024 Oct 17:107903. doi: 10.1016/j.jbc.2024.107903. PMID:39426727<ref>PMID:39426727</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8tg0" style="background-color:#fffaf0;"></div> |
| - | [[Category: Pinheiro | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Almeida FCL]] | ||
| + | [[Category: Pinheiro AS]] | ||
| + | [[Category: Pougy KC]] | ||
Current revision
Solution NMR structure of the cold shock domain of the Arabidopsis thaliana glycine-rich protein AtGRP2
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