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8J48

Crystal structure of OY phytoplasma SAP05 in complex with AtGATA18

Summary for 8J48
Entry DOI10.2210/pdb8j48/pdb
DescriptorGATA transcription factor 18, Sequence-variable mosaic (SVM) signal sequence domain-containing protein, ZINC ION, ... (4 entities in total)
Functional Keywordsubiquitin-independent protein degradation, plant protein
Biological sourceArabidopsis thaliana (thale cress)
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Total number of polymer chains4
Total formula weight36035.08
Authors
Dong, C.,Yan, X.,Yuan, X. (deposition date: 2023-04-19, release date: 2024-02-28, Last modification date: 2024-05-08)
Primary citationYan, X.,Yuan, X.,Lv, J.,Zhang, B.,Huang, Y.,Li, Q.,Ma, J.,Li, Y.,Wang, X.,Li, Y.,Yu, Y.,Liu, Q.,Liu, T.,Mi, W.,Dong, C.
Molecular basis of SAP05-mediated ubiquitin-independent proteasomal degradation of transcription factors.
Nat Commun, 15:1170-1170, 2024
Cited by
PubMed Abstract: SAP05, a secreted effector by the obligate parasitic bacteria phytoplasma, bridges host SPL and GATA transcription factors (TFs) to the 26 S proteasome subunit RPN10 for ubiquitination-independent degradation. Here, we report the crystal structures of SAP05 in complex with SPL5, GATA18 and RPN10, which provide detailed insights into the protein-protein interactions involving SAP05. SAP05 employs two opposing lobes with an acidic path and a hydrophobic path to contact TFs and RPN10, respectively. Our crystal structures, in conjunction with mutagenesis and degradation assays, reveal that SAP05 targets plant GATAs but not animal GATAs dependent on their direct salt-bridged electrostatic interactions. Additionally, SAP05 hijacks plant RPN10 but not animal RPN10 due to structural steric hindrance and the key hydrophobic interactions. This study provides valuable molecular-level information into the modulation of host proteins to prevent insect-borne diseases.
PubMed: 38326322
DOI: 10.1038/s41467-024-45521-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.94 Å)
Structure validation

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