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2P5Z

The E. coli c3393 protein is a component of the type VI secretion system and exhibits structural similarity to T4 bacteriophage tail proteins gp27 and gp5

Summary for 2P5Z
Entry DOI10.2210/pdb2p5z/pdb
DescriptorType VI secretion system component (2 entities in total)
Functional Keywordsstructural genomics, unknown function, psi-2, protein structure initiative, new york sgx research center for structural genomics, nysgxrc
Biological sourceEscherichia coli O6
Total number of polymer chains1
Total formula weight55697.99
Authors
Primary citationLeiman, P.G.,Basler, M.,Ramagopal, U.A.,Bonanno, J.B.,Sauder, J.M.,Pukatzki, S.,Burley, S.K.,Almo, S.C.,Mekalanos, J.J.
Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin.
Proc.Natl.Acad.Sci.Usa, 106:4154-4159, 2009
Cited by
PubMed Abstract: Protein secretion is a common property of pathogenic microbes. Gram-negative bacterial pathogens use at least 6 distinct extracellular protein secretion systems to export proteins through their multilayered cell envelope and in some cases into host cells. Among the most widespread is the newly recognized Type VI secretion system (T6SS) which is composed of 15-20 proteins whose biochemical functions are not well understood. Using crystallographic, biochemical, and bioinformatic analyses, we identified 3 T6SS components, which are homologous to bacteriophage tail proteins. These include the tail tube protein; the membrane-penetrating needle, situated at the distal end of the tube; and another protein associated with the needle and tube. We propose that T6SS is a multicomponent structure whose extracellular part resembles both structurally and functionally a bacteriophage tail, an efficient machine that translocates proteins and DNA across lipid membranes into cells.
PubMed: 19251641
DOI: 10.1073/pnas.0813360106
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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数据于2025-08-27公开中

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