7atp

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2.0 angstrom structure in complex with Ca of plant Extended Synaptotagmin 1, C2A domain

Structural highlights

7atp is a 1 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 2.1Å
Ligands:CA, CL, ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SYT1_ARATH Plays an important role in maintaining plasma membrane integrity during freezing and osmotic stresses. May function in membrane resealing during calcium-dependent freezing tolerance. May regulate endocytosis and endosome recycling at the plasma membrane and cell-to-cell trafficking of cabbage leaf curl virus (CaLCuV) and tobacco mosaic virus (TMV) movement proteins via plasmodesmata.[1] [2] [3] [4] [5]

Publication Abstract from PubMed

Non-vesicular lipid transfer at ER and plasma membrane (PM) contact sites (CS) is crucial for the maintenance of membrane lipid homeostasis. Extended synaptotagmins (E-Syts) play a central role in this process as they act as molecular tethers of ER and PM and as lipid transfer proteins between these organelles. E-Syts are proteins constitutively anchored to the ER through an N-terminal hydrophobic segment and bind the PM via a variable number of C-terminal C2 domains. Synaptotagmins (SYTs) are the plant orthologous of E-Syts and regulate the ER-PM communication in response to abiotic stress. Combining different structural and biochemical techniques, we demonstrate that the binding of SYT1 to lipids occurs through a Ca(2+)-dependent lipid-binding site and by a site for phosphorylated forms of phosphatidylinositol, thus integrating two different molecular signals in response to stress. In addition, we show that SYT1 displays three highly flexible hinge points that provide conformational freedom to facilitate lipid extraction, protein loading, and subsequent transfer between PM and ER.

The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites.,Benavente JL, Siliqi D, Infantes L, Lagartera L, Mills A, Gago F, Ruiz-Lopez N, Botella MA, Sanchez-Barrena MJ, Albert A Life Sci Alliance. 2021 Aug 18;4(10). pii: 4/10/e202101152. doi:, 10.26508/lsa.202101152. Print 2021 Oct. PMID:34408000[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
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Unbiased proteomic and forward genetic screens reveal that mechanosensitive ion channel MSL10 functions at ER-plasma membrane contact sites in <i>Arabidopsis thaliana</i>.
Codjoe et al. (2022)
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See Also

References

  1. ↑ Eckardt NA. Arabidopsis synaptotagmin1 maintains plasma membrane integrity. Plant Cell. 2008 Dec;20(12):3182. doi: 10.1105/tpc.108.201211. Epub 2008 Dec 16. PMID:19088328 doi:http://dx.doi.org/10.1105/tpc.108.201211
  2. ↑ Schapire AL, Voigt B, Jasik J, Rosado A, Lopez-Cobollo R, Menzel D, Salinas J, Mancuso S, Valpuesta V, Baluska F, Botella MA. Arabidopsis synaptotagmin 1 is required for the maintenance of plasma membrane integrity and cell viability. Plant Cell. 2008 Dec;20(12):3374-88. doi: 10.1105/tpc.108.063859. Epub 2008 Dec, 16. PMID:19088329 doi:http://dx.doi.org/10.1105/tpc.108.063859
  3. ↑ Yamazaki T, Kawamura Y, Minami A, Uemura M. Calcium-dependent freezing tolerance in Arabidopsis involves membrane resealing via synaptotagmin SYT1. Plant Cell. 2008 Dec;20(12):3389-404. doi: 10.1105/tpc.108.062679. Epub 2008 Dec , 16. PMID:19088330 doi:http://dx.doi.org/10.1105/tpc.108.062679
  4. ↑ Lewis JD, Lazarowitz SG. Arabidopsis synaptotagmin SYTA regulates endocytosis and virus movement protein cell-to-cell transport. Proc Natl Acad Sci U S A. 2010 Feb 9;107(6):2491-6. doi: 10.1073/pnas.0909080107., Epub 2010 Jan 21. PMID:20133785 doi:http://dx.doi.org/10.1073/pnas.0909080107
  5. ↑ Yamazaki T, Takata N, Uemura M, Kawamura Y. Arabidopsis synaptotagmin SYT1, a type I signal-anchor protein, requires tandem C2 domains for delivery to the plasma membrane. J Biol Chem. 2010 Jul 23;285(30):23165-76. doi: 10.1074/jbc.M109.084046. Epub, 2010 May 24. PMID:20498364 doi:http://dx.doi.org/10.1074/jbc.M109.084046
  6. ↑ Benavente JL, Siliqi D, Infantes L, Lagartera L, Mills A, Gago F, Ruiz-Lopez N, Botella MA, Sanchez-Barrena MJ, Albert A. The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites. Life Sci Alliance. 2021 Aug 18;4(10). pii: 4/10/e202101152. doi:, 10.26508/lsa.202101152. Print 2021 Oct. PMID:34408000 doi:http://dx.doi.org/10.26508/lsa.202101152

Contents


PDB ID 7atp

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