5a52: Difference between revisions
New page: '''Unreleased structure''' The entry 5a52 is ON HOLD Authors: Fernandez, D., Marquez, J.A. Description: The crystal structure of Arabidopsis thaliana CAR1 in complex with one calcium i... |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==The crystal structure of Arabidopsis thaliana CAR1 in complex with one calcium ion== | ||
<StructureSection load='5a52' size='340' side='right'caption='[[5a52]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5a52]] is a 1 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=5A52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A52 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5a52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a52 OCA], [https://pdbe.org/5a52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a52 RCSB], [https://www.ebi.ac.uk/pdbsum/5a52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a52 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAR1_ARATH CAR1_ARATH] Stimulates the GTPase/ATPase activities of Obg-like ATPases (By similarity). Mediates the transient calcium-dependent interaction of PYR/PYL/RCAR abscisic acid (ABA) receptors with the plasma membrane and thus regulates ABA sensitivity (PubMed:25465408).[UniProtKB:Q9LVH4]<ref>PMID:25465408</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Regulation of ion transport in plants is essential for cell function. Abiotic stress unbalances cell ion homeostasis, and plants tend to readjust it, regulating membrane transporters and channels. The plant hormone abscisic acid (ABA) and the second messenger Ca(2+) are central in such processes, as they are involved in the regulation of protein kinases and phosphatases that control ion transport activity in response to environmental stimuli. The identification and characterization of the molecular mechanisms underlying the effect of ABA and Ca(2+) signaling pathways on membrane function are central and could provide opportunities for crop improvement. The C2-domain ABA-related (CAR) family of small proteins is involved in the Ca(2+)-dependent recruitment of the pyrabactin resistance 1/PYR1-like (PYR/PYL) ABA receptors to the membrane. However, to fully understand CAR function, it is necessary to define a molecular mechanism that integrates Ca(2+) sensing, membrane interaction, and the recognition of the PYR/PYL interacting partners. We present structural and biochemical data showing that CARs are peripheral membrane proteins that functionally cluster on the membrane and generate strong positive membrane curvature in a Ca(2+)-dependent manner. These features represent a mechanism for the generation, stabilization, and/or specific recognition of membrane discontinuities. Such structures may act as signaling platforms involved in the recruitment of PYR/PYL receptors and other signaling components involved in cell responses to stress. | |||
Calcium-dependent oligomerization of CAR proteins at cell membrane modulates ABA signaling.,Diaz M, Sanchez-Barrena MJ, Gonzalez-Rubio JM, Rodriguez L, Fernandez D, Antoni R, Yunta C, Belda-Palazon B, Gonzalez-Guzman M, Peirats-Llobet M, Menendez M, Boskovic J, Marquez JA, Rodriguez PL, Albert A Proc Natl Acad Sci U S A. 2016 Jan 19;113(3):E396-405. doi:, 10.1073/pnas.1512779113. Epub 2015 Dec 30. PMID:26719420<ref>PMID:26719420</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5a52" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | |||
[[Category: Fernandez D]] | |||
[[Category: Marquez JA]] | |||
Latest revision as of 14:04, 10 January 2024
The crystal structure of Arabidopsis thaliana CAR1 in complex with one calcium ionThe crystal structure of Arabidopsis thaliana CAR1 in complex with one calcium ion
Structural highlights
FunctionCAR1_ARATH Stimulates the GTPase/ATPase activities of Obg-like ATPases (By similarity). Mediates the transient calcium-dependent interaction of PYR/PYL/RCAR abscisic acid (ABA) receptors with the plasma membrane and thus regulates ABA sensitivity (PubMed:25465408).[UniProtKB:Q9LVH4][1] Publication Abstract from PubMedRegulation of ion transport in plants is essential for cell function. Abiotic stress unbalances cell ion homeostasis, and plants tend to readjust it, regulating membrane transporters and channels. The plant hormone abscisic acid (ABA) and the second messenger Ca(2+) are central in such processes, as they are involved in the regulation of protein kinases and phosphatases that control ion transport activity in response to environmental stimuli. The identification and characterization of the molecular mechanisms underlying the effect of ABA and Ca(2+) signaling pathways on membrane function are central and could provide opportunities for crop improvement. The C2-domain ABA-related (CAR) family of small proteins is involved in the Ca(2+)-dependent recruitment of the pyrabactin resistance 1/PYR1-like (PYR/PYL) ABA receptors to the membrane. However, to fully understand CAR function, it is necessary to define a molecular mechanism that integrates Ca(2+) sensing, membrane interaction, and the recognition of the PYR/PYL interacting partners. We present structural and biochemical data showing that CARs are peripheral membrane proteins that functionally cluster on the membrane and generate strong positive membrane curvature in a Ca(2+)-dependent manner. These features represent a mechanism for the generation, stabilization, and/or specific recognition of membrane discontinuities. Such structures may act as signaling platforms involved in the recruitment of PYR/PYL receptors and other signaling components involved in cell responses to stress. Calcium-dependent oligomerization of CAR proteins at cell membrane modulates ABA signaling.,Diaz M, Sanchez-Barrena MJ, Gonzalez-Rubio JM, Rodriguez L, Fernandez D, Antoni R, Yunta C, Belda-Palazon B, Gonzalez-Guzman M, Peirats-Llobet M, Menendez M, Boskovic J, Marquez JA, Rodriguez PL, Albert A Proc Natl Acad Sci U S A. 2016 Jan 19;113(3):E396-405. doi:, 10.1073/pnas.1512779113. Epub 2015 Dec 30. PMID:26719420[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||