4Z94
Actin Complex With a Chimera of Tropomodulin-1 and Leiomodin-1 Actin-Binding Site 2
Summary for 4Z94
| Entry DOI | 10.2210/pdb4z94/pdb |
| Related | 4Z8G |
| Descriptor | Actin, alpha skeletal muscle, Gelsolin, Tropomodulin-1, Leiomodin-1 chimera, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | actin nucleator, atp-actin, protein binding-structural protein complex, protein binding/structural protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 79270.84 |
| Authors | Rebowski, G.,Boczkowska, M.,Dominguez, R. (deposition date: 2015-04-09, release date: 2015-10-21, Last modification date: 2023-09-27) |
| Primary citation | Boczkowska, M.,Rebowski, G.,Kremneva, E.,Lappalainen, P.,Dominguez, R. How Leiomodin and Tropomodulin use a common fold for different actin assembly functions. Nat Commun, 6:8314-8314, 2015 Cited by PubMed Abstract: How proteins sharing a common fold have evolved different functions is a fundamental question in biology. Tropomodulins (Tmods) are prototypical actin filament pointed-end-capping proteins, whereas their homologues, Leiomodins (Lmods), are powerful filament nucleators. We show that Tmods and Lmods do not compete biochemically, and display similar but distinct localization in sarcomeres. Changes along the polypeptide chains of Tmods and Lmods exquisitely adapt their functions for capping versus nucleation. Tmods have alternating tropomyosin (TM)- and actin-binding sites (TMBS1, ABS1, TMBS2 and ABS2). Lmods additionally contain a C-terminal extension featuring an actin-binding WH2 domain. Unexpectedly, the different activities of Tmods and Lmods do not arise from the Lmod-specific extension. Instead, nucleation by Lmods depends on two major adaptations-the loss of pointed-end-capping elements present in Tmods and the specialization of the highly conserved ABS2 for recruitment of two or more actin subunits. The WH2 domain plays only an auxiliary role in nucleation. PubMed: 26370058DOI: 10.1038/ncomms9314 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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