3CJC

Actin dimer cross-linked by V. cholerae MARTX toxin and complexed with DNase I and Gelsolin-segment 1

Summary for 3CJC

• Entry DOI: 10.2210/pdb3cjc/pdb
• Related: 3CJB
• Descriptor: Actin, alpha skeletal muscle, Deoxyribonuclease-1, Gelsolin, ... (8 entities in total)
• Functional Keywords: cross-linked dimer, atp-binding, cytoskeleton, methylation, muscle protein, nucleotide-binding, phosphoprotein, structural protein, actin-binding, apoptosis, endonuclease, glycoprotein, hydrolase, nuclease, nucleus, secreted, actin capping, alternative initiation, amyloid, disease mutation, structural protein-hydrolase complex, structural protein/hydrolase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 86849.47

Authors

Sawaya, M.R.,Kudryashov, D.S.,Pashkov, I.,Reisler, E.,Yeates, T.O. (deposition date: 2008-03-12, release date: 2008-03-25, Last modification date: 2020-07-29)

• Primary citation: Kudryashov, D.S.,Durer, Z.A.,Ytterberg, A.J.,Sawaya, M.R.,Pashkov, I.,Prochazkova, K.,Yeates, T.O.,Loo, R.R.,Loo, J.A.,Satchell, K.J.,Reisler, E.; Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin.; Proc.Natl.Acad.Sci.USA, 105:18537-18542, 2008; PubMed: 19015515; DOI: 10.1073/pnas.0808082105

Experimental method

X-RAY DIFFRACTION (3.9 Å)