2gwj

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SpvB ADP-ribosylated actin: hexagonal crystal formSpvB ADP-ribosylated actin: hexagonal crystal form

Structural highlights

2gwj is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Publication Abstract from PubMed

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.

A steric antagonism of actin polymerization by a salmonella virulence protein.,Margarit SM, Davidson W, Frego L, Stebbins CE Structure. 2006 Aug;14(8):1219-29. PMID:16905096[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Margarit SM, Davidson W, Frego L, Stebbins CE. A steric antagonism of actin polymerization by a salmonella virulence protein. Structure. 2006 Aug;14(8):1219-29. PMID:16905096 doi:10.1016/j.str.2006.05.022

2gwj, resolution 1.90Å

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OCA