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2J9T

BipD of Burkholderia Pseudomallei

Replaces:  2CMQ
Summary for 2J9T
Entry DOI10.2210/pdb2j9t/pdb
Related2IXR 2IZP
DescriptorMEMBRANE ANTIGEN, BORIC ACID, CITRATE ANION, ... (4 entities in total)
Functional Keywordsburkholderia pseudomallei, bipd, ttss, t3ss, type 3 secretion system, toxin
Biological sourceBURKHOLDERIA PSEUDOMALLEI
Cellular locationSecreted : Q63K37
Total number of polymer chains2
Total formula weight66487.20
Authors
Johnson, S.,Roversi, P.,Field, T.,Deane, J.E.,Galyov, E.,Lea, S.M. (deposition date: 2006-11-16, release date: 2006-11-20, Last modification date: 2024-05-08)
Primary citationJohnson, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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