6LAG
Solution structure of SPA-2 SHD
Summary for 6LAG
| Entry DOI | 10.2210/pdb6lag/pdb |
| NMR Information | BMRB: 36299 |
| Descriptor | Spa2-like protein (1 entity in total) |
| Functional Keywords | shd, spa-2, git-pix, polarity, signaling protein |
| Biological source | Neurospora crassa |
| Total number of polymer chains | 1 |
| Total formula weight | 17781.94 |
| Authors | Fan, J.S.,Wong, J.Y.,Zheng, P.,Yang, D.,Jedd, G. (deposition date: 2019-11-12, release date: 2020-04-29, Last modification date: 2024-05-15) |
| Primary citation | Zheng, P.,Nguyen, T.A.,Wong, J.Y.,Lee, M.,Nguyen, T.A.,Fan, J.S.,Yang, D.,Jedd, G. Spitzenkorper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds. Nat Commun, 11:2830-2830, 2020 Cited by PubMed Abstract: The Spitzenkörper (SPK) constitutes a collection of secretory vesicles and polarity-related proteins intimately associated with polarized growth of fungal hyphae. Many SPK-localized proteins are known, but their assembly and dynamics remain poorly understood. Here, we identify protein-protein interaction cascades leading to assembly of two SPK scaffolds and recruitment of diverse effectors in Neurospora crassa. Both scaffolds are transported to the SPK by the myosin V motor (MYO-5), with the coiled-coil protein SPZ-1 acting as cargo adaptor. Neither scaffold appears to be required for accumulation of SPK secretory vesicles. One scaffold consists of Leashin-2 (LAH-2), which is required for SPK localization of the signalling kinase COT-1 and the glycolysis enzyme GPI-1. The other scaffold comprises a complex of Janus-1 (JNS-1) and the polarisome protein SPA-2. Via its Spa homology domain (SHD), SPA-2 recruits a calponin domain-containing F-actin effector (CCP-1). The SHD NMR structure reveals a conserved surface groove required for effector binding. Similarities between SPA-2/JNS-1 and the metazoan GIT/PIX complex identify foundational features of the cell polarity apparatus that predate the fungal-metazoan divergence. PubMed: 32503980DOI: 10.1038/s41467-020-16712-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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