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8JTK

Structure of AYWB phytoplasma SAP05 recognizing AtRpn10

Summary for 8JTK
Entry DOI10.2210/pdb8jtk/pdb
Descriptor26S proteasome non-ATPase regulatory subunit 4 homolog, Sequence-variable mosaic (SVM) signal sequence domain-containing protein (3 entities in total)
Functional Keywordscomplex, proteasome, hijack, plant protein
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains2
Total formula weight33190.75
Authors
Du, Y.X.,Zhang, L.Y.,Zheng, Q.Y. (deposition date: 2023-06-22, release date: 2023-07-19, Last modification date: 2024-07-17)
Primary citationZhang, L.,Du, Y.,Qu, Q.,Zheng, Q.
Structure basis for recognition of plant Rpn10 by phytoplasma SAP05 in ubiquitin-independent protein degradation.
Iscience, 27:108892-108892, 2024
Cited by
PubMed Abstract: Besides traditional ubiquitin-dependent proteasome degradation, thousands of eukaryotic proteins more than previously appreciated could undergo ubiquitin-independent proteasomal degradation (UbInPD). A pathogen-encoded effector protein SAP05 secreted by phytoplasma, could hijack hostage Rpn10 subunit of proteasome derived from and target the degradation of GATA BINDING FACTOR (GATA) or SQUAMOSA-PROMOTER BINDING PROTEIN-LIKE (SPL) transcription factors (TFs) without ubiquitin or additional proteasome shuttle factors. To explain how could SAP05 target the degradation bypassing the ubiquitin-dependent pathway, we have determined the crystal structure of the complex between Rpn10 and SAP05 or SAP05, which showed a previously unknown recognition interface. Sequence alignment and structural biological evidence showed that this interaction is highly conserved in various SAP05 homologs, suggesting a general mode in plant infection. After docking the complex structure to the plant proteasome, SAP05 was near to the adenosine triphosphatase (ATPase) central pore and enough to submit substrate to degradation process, which suggested a molecular glue-like role to bridge TFs close to the ATPase central pore of proteasomes for the direct degradation.
PubMed: 38322988
DOI: 10.1016/j.isci.2024.108892
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.57 Å)
Structure validation

237992

数据于2025-06-25公开中

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