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4RL5

Crystal structure of the Arabidopsis exocyst subunit exo70 family protein A1

Summary for 4RL5
Entry DOI10.2210/pdb4rl5/pdb
DescriptorExocyst complex component EXO70A1 (1 entity in total)
Functional Keywordsexocyst complex, protein binding
Biological sourceArabidopsis thaliana (mouse-ear cress,thale-cress)
Cellular locationCytoplasm, cytosol : Q9LZD3
Total number of polymer chains2
Total formula weight129761.18
Authors
Zhang, Z.-M.,Zhang, C.,Song, J. (deposition date: 2014-10-15, release date: 2015-11-25, Last modification date: 2024-10-16)
Primary citationZhang, C.,Brown, M.Q.,van de Ven, W.,Zhang, Z.M.,Wu, B.,Young, M.C.,Synek, L.,Borchardt, D.,Harrison, R.,Pan, S.,Luo, N.,Huang, Y.M.,Ghang, Y.J.,Ung, N.,Li, R.,Isley, J.,Morikis, D.,Song, J.,Guo, W.,Hooley, R.J.,Chang, C.E.,Yang, Z.,Zarsky, V.,Muday, G.K.,Hicks, G.R.,Raikhel, N.V.
Endosidin2 targets conserved exocyst complex subunit EXO70 to inhibit exocytosis.
Proc.Natl.Acad.Sci.USA, 113:E41-E50, 2016
Cited by
PubMed Abstract: The exocyst complex regulates the last steps of exocytosis, which is essential to organisms across kingdoms. In humans, its dysfunction is correlated with several significant diseases, such as diabetes and cancer progression. Investigation of the dynamic regulation of the evolutionarily conserved exocyst-related processes using mutants in genetically tractable organisms such as Arabidopsis thaliana is limited by the lethality or the severity of phenotypes. We discovered that the small molecule Endosidin2 (ES2) binds to the EXO70 (exocyst component of 70 kDa) subunit of the exocyst complex, resulting in inhibition of exocytosis and endosomal recycling in both plant and human cells and enhancement of plant vacuolar trafficking. An EXO70 protein with a C-terminal truncation results in dominant ES2 resistance, uncovering possible distinct regulatory roles for the N terminus of the protein. This study not only provides a valuable tool in studying exocytosis regulation but also offers a potentially new target for drugs aimed at addressing human disease.
PubMed: 26607451
DOI: 10.1073/pnas.1521248112
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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