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7C1M

Complex structure of tyrosinated alpha-tubulin carboxy-terminal peptide and A1aY1 binder

Summary for 7C1M
Entry DOI10.2210/pdb7c1m/pdb
DescriptorNanobody binder from SSO7d library, Carboxy-terminal peptide from tyrosinated alpha-tubulin (2 entities in total)
Functional Keywordstyrosinated, microtubule, binder, sso7d, yeast display, protein binding
Biological sourceSaccharolobus solfataricus 98/2
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Total number of polymer chains2
Total formula weight8842.13
Authors
Kesarwani, S.,Reddy, P.P.,Sirajuddin, M.,Das, R. (deposition date: 2020-05-05, release date: 2020-09-02, Last modification date: 2024-05-15)
Primary citationKesarwani, S.,Lama, P.,Chandra, A.,Reddy, P.P.,Jijumon, A.S.,Bodakuntla, S.,Rao, B.M.,Janke, C.,Das, R.,Sirajuddin, M.
Genetically encoded live-cell sensor for tyrosinated microtubules.
J.Cell Biol., 219:-, 2020
Cited by
PubMed Abstract: Microtubule cytoskeleton exists in various biochemical forms in different cells due to tubulin posttranslational modifications (PTMs). Tubulin PTMs are known to affect microtubule stability, dynamics, and interaction with MAPs and motors in a specific manner, widely known as tubulin code hypothesis. At present, there exists no tool that can specifically mark tubulin PTMs in living cells, thus severely limiting our understanding of their dynamics and cellular functions. Using a yeast display library, we identified a binder against terminal tyrosine of α-tubulin, a unique PTM site. Extensive characterization validates the robustness and nonperturbing nature of our binder as tyrosination sensor, a live-cell tubulin nanobody specific towards tyrosinated microtubules. Using this sensor, we followed nocodazole-, colchicine-, and vincristine-induced depolymerization events of tyrosinated microtubules in real time and found each distinctly perturbs the microtubule polymer. Together, our work describes a novel tyrosination sensor and its potential applications to study the dynamics of microtubule and their PTM processes in living cells.
PubMed: 32886100
DOI: 10.1083/jcb.201912107
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

237992

数据于2025-06-25公开中

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