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2GWJ

SpvB ADP-ribosylated actin: hexagonal crystal form

Summary for 2GWJ
Entry DOI10.2210/pdb2gwj/pdb
Related2GWK
DescriptorActin, alpha skeletal muscle, CALCIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
Functional Keywordsactin, adp-ribosylation, contractile protein
Biological sourceOryctolagus cuniculus (rabbit)
Cellular locationCytoplasm, cytoskeleton: P68135
Total number of polymer chains1
Total formula weight41934.49
Authors
Stebbins, C.E.,Margarit, S.M. (deposition date: 2006-05-04, release date: 2006-08-29, Last modification date: 2017-10-18)
Primary citationMargarit, 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: 16905096
DOI: 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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