2GWJ
SpvB ADP-ribosylated actin: hexagonal crystal form
Summary for 2GWJ
Entry DOI | 10.2210/pdb2gwj/pdb |
Related | 2GWK |
Descriptor | Actin, alpha skeletal muscle, CALCIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | actin, adp-ribosylation, contractile protein |
Biological source | Oryctolagus cuniculus (rabbit) |
Cellular location | Cytoplasm, cytoskeleton: P68135 |
Total number of polymer chains | 1 |
Total formula weight | 41934.49 |
Authors | Stebbins, C.E.,Margarit, S.M. (deposition date: 2006-05-04, release date: 2006-08-29, Last modification date: 2017-10-18) |
Primary citation | Margarit, S.M.,Davidson, W.,Frego, L.,Stebbins, C.E. A steric antagonism of actin polymerization by a salmonella virulence protein. Structure, 14:1219-1229, 2006 Cited by PubMed Abstract: Salmonella spp. require the ADP-ribosyltransferase activity of the SpvB protein for intracellular growth and systemic virulence. SpvB covalently modifies actin, causing cytoskeletal disruption and apoptosis. We report here the crystal structure of the catalytic domain of SpvB, and we show by mass spectrometric analysis that SpvB modifies actin at Arg177, inhibiting its ATPase activity. We also describe two crystal structures of SpvB-modified, polymerization-deficient actin. These structures reveal that ADP-ribosylation does not lead to dramatic conformational changes in actin, suggesting a model in which this large family of toxins inhibits actin polymerization primarily through steric disruption of intrafilament contacts. PubMed: 16905096DOI: 10.1016/j.str.2006.05.022 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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