2GWK

SpvB ADP-ribosylated actin: orthorhombic crystal form

Summary for 2GWK

• Entry DOI: 10.2210/pdb2gwk/pdb
• Related: 2GWJ
• 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: 2
• Total formula weight: 83868.97

Authors

Stebbins, C.E.,Margarit, S.M. (deposition date: 2006-05-04, release date: 2006-08-29, Last modification date: 2011-07-13)

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

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: 16905096
DOI: 10.1016/j.str.2006.05.022

Experimental method

X-RAY DIFFRACTION (2 Å)