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| - | [[Image:2xtz.png|left|200px]] | |
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| - | <!-- | + | ==Crystal structure of the G alpha protein AtGPA1 from Arabidopsis thaliana== |
| - | The line below this paragraph, containing "STRUCTURE_2xtz", creates the "Structure Box" on the page.
| + | <StructureSection load='2xtz' size='340' side='right'caption='[[2xtz]], [[Resolution|resolution]] 2.34Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | + | <table><tr><td colspan='2'>[[2xtz]] is a 3 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=2XTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XTZ FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34Å</td></tr> |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | {{STRUCTURE_2xtz| PDB=2xtz | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xtz OCA], [https://pdbe.org/2xtz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xtz RCSB], [https://www.ebi.ac.uk/pdbsum/2xtz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xtz ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GPA1_ARATH GPA1_ARATH] Exhibits a fast rate of basal nucleotide exchange. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Together with GCR1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector and inositol 1,4,5-trisphosphate(IP(3)) as a second messenger. Promotes abscisic acid (ABA) responses in guard cells. But, together with GCR1 and GB1, acts as a negative regulator of ABA during seed germination and early seedling development. Involved in the blue light (BL) signaling. Together with GCR1 and ADT3, required for BL-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Modulates root architecture (e.g. lateral root formation). Negatively regulated by RGS1.<ref>PMID:15155892</ref> <ref>PMID:16415218</ref> <ref>PMID:16581874</ref> <ref>PMID:17322342</ref> <ref>PMID:20862254</ref> <ref>PMID:21304159</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | In animals, heterotrimeric guanine nucleotide-binding protein (G protein) signaling is initiated by G protein-coupled receptors (GPCRs), which activate G protein alpha subunits; however, the plant Arabidopsis thaliana lacks canonical GPCRs, and its G protein alpha subunit (AtGPA1) is self-activating. To investigate how AtGPA1 becomes activated, we determined its crystal structure. AtGPA1 is structurally similar to animal G protein alpha subunits, but our crystallographic and biophysical studies revealed that it had distinct properties. Notably, the helical domain of AtGPA1 displayed pronounced intrinsic disorder and a tendency to disengage from the Ras domain of the protein. Domain substitution experiments showed that the helical domain of AtGPA1 was necessary for self-activation and sufficient to confer self-activation to an animal G protein alpha subunit. These findings reveal the structural basis for a mechanism for G protein activation in Arabidopsis that is distinct from the well-established mechanism found in animals. |
| | | | |
| - | ===CRYSTAL STRUCTURE OF THE G ALPHA PROTEIN ATGPA1 FROM ARABIDOPSIS THALIANA===
| + | The crystal structure of a self-activating G protein {alpha} subunit reveals its distinct mechanism of signal initiation.,Jones JC, Duffy JW, Machius M, Temple BR, Dohlman HG, Jones AM Sci Signal. 2011 Feb 8;4(159):ra8. PMID:21304159<ref>PMID:21304159</ref> |
| | | | |
| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <!--
| + | </div> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_21304159}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 2xtz" style="background-color:#fffaf0;"></div> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 21304159 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_21304159}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | |
| - | [[2xtz]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XTZ OCA].
| + | |
| - | | + | |
| - | ==Reference== | + | |
| - | <ref group="xtra">PMID:21304159</ref><ref group="xtra">PMID:17951432</ref><references group="xtra"/> | + | |
| | [[Category: Arabidopsis thaliana]] | | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Heterotrimeric G-protein GTPase]] | + | [[Category: Large Structures]] |
| - | [[Category: Dohlman, H G.]] | + | [[Category: Dohlman HG]] |
| - | [[Category: Duffy, J W.]] | + | [[Category: Duffy JW]] |
| - | [[Category: Jones, A M.]] | + | [[Category: Jones AM]] |
| - | [[Category: Jones, J C.]] | + | [[Category: Jones JC]] |
| - | [[Category: Machius, M.]] | + | [[Category: Machius M]] |
| - | [[Category: Temple, B R.S.]] | + | [[Category: Temple BRS]] |
| Structural highlights
2xtz is a 3 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.34Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
GPA1_ARATH Exhibits a fast rate of basal nucleotide exchange. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Together with GCR1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector and inositol 1,4,5-trisphosphate(IP(3)) as a second messenger. Promotes abscisic acid (ABA) responses in guard cells. But, together with GCR1 and GB1, acts as a negative regulator of ABA during seed germination and early seedling development. Involved in the blue light (BL) signaling. Together with GCR1 and ADT3, required for BL-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Modulates root architecture (e.g. lateral root formation). Negatively regulated by RGS1.[1] [2] [3] [4] [5] [6]
Publication Abstract from PubMed
In animals, heterotrimeric guanine nucleotide-binding protein (G protein) signaling is initiated by G protein-coupled receptors (GPCRs), which activate G protein alpha subunits; however, the plant Arabidopsis thaliana lacks canonical GPCRs, and its G protein alpha subunit (AtGPA1) is self-activating. To investigate how AtGPA1 becomes activated, we determined its crystal structure. AtGPA1 is structurally similar to animal G protein alpha subunits, but our crystallographic and biophysical studies revealed that it had distinct properties. Notably, the helical domain of AtGPA1 displayed pronounced intrinsic disorder and a tendency to disengage from the Ras domain of the protein. Domain substitution experiments showed that the helical domain of AtGPA1 was necessary for self-activation and sufficient to confer self-activation to an animal G protein alpha subunit. These findings reveal the structural basis for a mechanism for G protein activation in Arabidopsis that is distinct from the well-established mechanism found in animals.
The crystal structure of a self-activating G protein {alpha} subunit reveals its distinct mechanism of signal initiation.,Jones JC, Duffy JW, Machius M, Temple BR, Dohlman HG, Jones AM Sci Signal. 2011 Feb 8;4(159):ra8. PMID:21304159[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pandey S, Assmann SM. The Arabidopsis putative G protein-coupled receptor GCR1 interacts with the G protein alpha subunit GPA1 and regulates abscisic acid signaling. Plant Cell. 2004 Jun;16(6):1616-32. Epub 2004 May 21. PMID:15155892 doi:http://dx.doi.org/10.1105/tpc.020321
- ↑ Warpeha KM, Lateef SS, Lapik Y, Anderson M, Lee BS, Kaufman LS. G-protein-coupled receptor 1, G-protein Galpha-subunit 1, and prephenate dehydratase 1 are required for blue light-induced production of phenylalanine in etiolated Arabidopsis. Plant Physiol. 2006 Mar;140(3):844-55. Epub 2006 Jan 13. PMID:16415218 doi:http://dx.doi.org/10.1104/pp.105.071282
- ↑ Pandey S, Chen JG, Jones AM, Assmann SM. G-protein complex mutants are hypersensitive to abscisic acid regulation of germination and postgermination development. Plant Physiol. 2006 May;141(1):243-56. Epub 2006 Mar 31. PMID:16581874 doi:http://dx.doi.org/pp.106.079038
- ↑ Warpeha KM, Upadhyay S, Yeh J, Adamiak J, Hawkins SI, Lapik YR, Anderson MB, Kaufman LS. The GCR1, GPA1, PRN1, NF-Y signal chain mediates both blue light and abscisic acid responses in Arabidopsis. Plant Physiol. 2007 Apr;143(4):1590-600. Epub 2007 Feb 23. PMID:17322342 doi:http://dx.doi.org/10.1104/pp.106.089904
- ↑ Booker KS, Schwarz J, Garrett MB, Jones AM. Glucose attenuation of auxin-mediated bimodality in lateral root formation is partly coupled by the heterotrimeric G protein complex. PLoS One. 2010 Sep 17;5(9). pii: e12833. doi: 10.1371/journal.pone.0012833. PMID:20862254 doi:http://dx.doi.org/10.1371/journal.pone.0012833
- ↑ Jones JC, Duffy JW, Machius M, Temple BR, Dohlman HG, Jones AM. The crystal structure of a self-activating G protein {alpha} subunit reveals its distinct mechanism of signal initiation. Sci Signal. 2011 Feb 8;4(159):ra8. PMID:21304159 doi:10.1126/scisignal.2001446
- ↑ Jones JC, Duffy JW, Machius M, Temple BR, Dohlman HG, Jones AM. The crystal structure of a self-activating G protein {alpha} subunit reveals its distinct mechanism of signal initiation. Sci Signal. 2011 Feb 8;4(159):ra8. PMID:21304159 doi:10.1126/scisignal.2001446
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