2JAA

SeMet substituted Shigella Flexneri Ipad

Summary for 2JAA

• Entry DOI: 10.2210/pdb2jaa/pdb
• Related: 2J0N 2J0O
• Descriptor: INVASIN IPAD (2 entities in total)
• Functional Keywords: ipad, t3ss, semet, invasin, virulence, cell invasion, shigella flexneri, type iii secretion
• Biological source: SHIGELLA FLEXNERI
• Cellular location: Secreted : P18013
• Total number of polymer chains: 2
• Total formula weight: 47479.38

Authors

Johnson, S.,Roversi, P.,Espina, M.,Olive, A.,Deane, J.E.,Birket, S.,Field, T.,Picking, W.D.,Blocker, A.J.,Galyov, E.E.,Picking, W.L.,Lea, S.M. (deposition date: 2006-11-24, release date: 2006-11-30, Last modification date: 2017-06-28)

Primary citation

Johnson, S.,Roversi, P.,Espina, M.,Olive, A.,Deane, J.E.,Birket, S.,Field, T.,Picking, W.D.,Blocker, A.J.,Galyov, E.E.,Picking, W.L.,Lea, S.M.
Self-Chaperoning of the Type III Secretion System Needle Tip Proteins Ipad and Bipd.
J.Biol.Chem., 282:4035-, 2007

PubMed Abstract: Bacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. The T3SS is composed of a basal body, which traverses both bacterial membranes, and an external needle through which effector proteins are secreted. We report multiple crystal structures of two proteins that sit at the tip of the needle and are essential for virulence: IpaD from Shigella flexneri and BipD from Burkholderia pseudomallei. The structures reveal that the N-terminal domains of the molecules are intramolecular chaperones that prevent premature oligomerization, as well as sharing structural homology with proteins involved in eukaryotic actin rearrangement. Crystal packing has allowed us to construct a model for the tip complex that is supported by mutations designed using the structure.

PubMed: 17077085
DOI: 10.1074/JBC.M607945200

Experimental method

X-RAY DIFFRACTION (3.1 Å)