2D8B

Solution structure of the second tandem cofilin-domain of mouse twinfilin

Summary for 2D8B

• Entry DOI: 10.2210/pdb2d8b/pdb
• Descriptor: Twinfilin-1 (1 entity in total)
• Functional Keywords: cell-free protein synthesis, actin-binding protein, developmental regulation, cellular remodeling, cytoskeleton, morphology, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, protein binding
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm: Q91YR1
• Total number of polymer chains: 1
• Total formula weight: 18889.19

Authors

Goroncy, A.K.,Kigawa, T.,Koshiba, S.,Sato, M.,Kobayashi, N.,Tochio, N.,Inoue, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-12-02, release date: 2006-06-02, Last modification date: 2024-05-29)

Primary citation

Goroncy, A.K.,Koshiba, S.,Tochio, N.,Tomizawa, T.,Sato, M.,Inoue, M.,Watanabe, S.,Hayashizaki, Y.,Tanaka, A.,Kigawa, T.,Yokoyama, S.
NMR solution structures of actin depolymerizing factor homology domains
Protein Sci., 18:2384-2392, 2009

PubMed Abstract: Actin is one of the most conserved proteins in nature. Its assembly and disassembly are regulated by many proteins, including the family of actin-depolymerizing factor homology (ADF-H) domains. ADF-H domains can be divided into five classes: ADF/cofilin, glia maturation factor (GMF), coactosin, twinfilin, and Abp1/drebrin. The best-characterized class is ADF/cofilin. The other four classes have drawn much less attention and very few structures have been reported. This study presents the solution NMR structure of the ADF-H domain of human HIP-55-drebrin-like protein, the first published structure of a drebrin-like domain (mammalian), and the first published structure of GMF beta (mouse). We also determined the structures of mouse GMF gamma, the mouse coactosin-like domain and the C-terminal ADF-H domain of mouse twinfilin 1. Although the overall fold of the five domains is similar, some significant differences provide valuable insights into filamentous actin (F-actin) and globular actin (G-actin) binding, including the identification of binding residues on the long central helix. This long helix is stabilized by three or four residues. Notably, the F-actin binding sites of mouse GMF beta and GMF gamma contain two additional beta-strands not seen in other ADF-H structures. The G-actin binding site of the ADF-H domain of human HIP-55-drebrin-like protein is absent and distorted in mouse GMF beta and GMF gamma.

PubMed: 19768801
DOI: 10.1002/pro.248

Experimental method

SOLUTION NMR