2xtz

From Proteopedia

(Difference between revisions)

Revision as of 14:54, 17 November 2021

Crystal structure of the G alpha protein AtGPA1 from Arabidopsis thaliana

Structural highlights

2xtz is a 3 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
NonStd Res:
Activity:	Heterotrimeric G-protein GTPase, with EC number 3.6.5.1
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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xtz"

@@ Line 3: / Line 3: @@
 <StructureSection load='2xtz' size='340' side='right'caption='[[2xtz]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xtz]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XTZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xtz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. 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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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>
+</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=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>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heterotrimeric_G-protein_GTPase Heterotrimeric G-protein GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.1 3.6.5.1] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Heterotrimeric_G-protein_GTPase Heterotrimeric G-protein GTPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.1 3.6.5.1] </span></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=2xtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xtz OCA], [http://pdbe.org/2xtz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xtz RCSB], [http://www.ebi.ac.uk/pdbsum/2xtz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xtz ProSAT]</span></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=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 ==
-[[http://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>
+[[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 ==

2xtz

From Proteopedia

Revision as of 14:54, 17 November 2021

Crystal structure of the G alpha protein AtGPA1 from Arabidopsis thaliana

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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