1QZ5

Structure of rabbit actin in complex with kabiramide C

Summary for 1QZ5

• Entry DOI: 10.2210/pdb1qz5/pdb
• Related: 1QZ6
• Descriptor: Actin, alpha skeletal muscle, CALCIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: actin, trisoxazole, toxin, kabiramide c, structural protein
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Cytoplasm, cytoskeleton: P68135
• Total number of polymer chains: 1
• Total formula weight: 43369.03

Authors

Klenchin, V.A.,Allingham, J.S.,King, R.,Tanaka, J.,Marriott, G.,Rayment, I. (deposition date: 2003-09-15, release date: 2003-11-11, Last modification date: 2025-03-26)

Primary citation

Klenchin, V.A.,Allingham, J.S.,King, R.,Tanaka, J.,Marriott, G.,Rayment, I.
Trisoxazole macrolide toxins mimic the binding of actin-capping proteins to actin
Nat.Struct.Biol., 10:1058-1063, 2003

PubMed Abstract: Marine macrolide toxins of trisoxazole family target actin with high affinity and specificity and have promising pharmacological properties. We present X-ray structures of actin in complex with two members of this family, kabiramide C and jaspisamide A, at a resolution of 1.45 and 1.6 A, respectively. The structures reveal the absolute stereochemistry of these toxins and demonstrate that their trisoxazole ring interacts with actin subdomain 1 while the aliphatic side chain is inserted into the hydrophobic cavity between actin subdomains 1 and 3. The binding site is essentially the same as the one occupied by the actin-capping domain of the gelsolin superfamily of proteins. The structural evidence suggests that actin filament severing and capping by these toxins is also analogous to that of gelsolin. Consequently, these macrolides may be viewed as small molecule biomimetics of an entire class of actin-binding proteins.

PubMed: 14578936
DOI: 10.1038/nsb1006

Experimental method

X-RAY DIFFRACTION (1.45 Å)