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 Cited by PubMed: 19015515DOI: 10.1073/pnas.0808082105 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.9 Å) |
Structure validation
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