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3TU3

1.92 Angstrom resolution crystal structure of the full-length SpcU in complex with full-length ExoU from the type III secretion system of Pseudomonas aeruginosa

Summary for 3TU3
Entry DOI10.2210/pdb3tu3/pdb
DescriptorExoU chaperone, ExoU (3 entities in total)
Functional Keywordstype iii secretion system, pseudomonas aeruginosa, exou, spcu, infectious diseases, structural genomics, center for structural genomics of infectious diseases, csgid, spcu- chaperone, exou - phospholipase a2, toxin-toxin chaperone complex, toxin/toxin chaperone
Biological sourcePseudomonas aeruginosa
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Total number of polymer chains2
Total formula weight94438.66
Authors
Primary citationHalavaty, A.S.,Borek, D.,Tyson, G.H.,Veesenmeyer, J.L.,Shuvalova, L.,Minasov, G.,Otwinowski, Z.,Hauser, A.R.,Anderson, W.F.
Structure of the Type III Secretion Effector Protein ExoU in Complex with Its Chaperone SpcU.
Plos One, 7:e49388-e49388, 2012
Cited by
PubMed Abstract: Disease causing bacteria often manipulate host cells in a way that facilitates the infectious process. Many pathogenic gram-negative bacteria accomplish this by using type III secretion systems. In these complex secretion pathways, bacterial chaperones direct effector proteins to a needle-like secretion apparatus, which then delivers the effector protein into the host cell cytosol. The effector protein ExoU and its chaperone SpcU are components of the Pseudomonas aeruginosa type III secretion system. Secretion of ExoU has been associated with more severe infections in both humans and animal models. Here we describe the 1.92 Å X-ray structure of the ExoU-SpcU complex, a full-length type III effector in complex with its full-length cognate chaperone. Our crystallographic data allow a better understanding of the mechanism by which ExoU kills host cells and provides a foundation for future studies aimed at designing inhibitors of this potent toxin.
PubMed: 23166655
DOI: 10.1371/journal.pone.0049388
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.92 Å)
Structure validation

237992

数据于2025-06-25公开中

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