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4ACK

3D Structure of DotU from Francisella novicida

Summary for 4ACK
Entry DOI10.2210/pdb4ack/pdb
Related4ACL
DescriptorTSSL, BROMIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsprotein transport, t6ss, microbial surface structures, virulence factor
Biological sourceFRANCISELLA NOVICIDA
Total number of polymer chains2
Total formula weight44966.26
Authors
Robb, C.S.,Nano, F.E.,Boraston, A.B. (deposition date: 2011-12-15, release date: 2012-04-25, Last modification date: 2024-05-08)
Primary citationRobb, C.S.,Nano, F.E.,Boraston, A.B.
The Structure of the Conserved Type Six Secretion Protein Tssl (Dotu) from Francisella Novicida
J.Mol.Biol., 419:277-, 2012
Cited by
PubMed Abstract: Type six secretion systems (T6SSs) are found in many Gram-negative bacteria and are important for their virulence or their ecological competitiveness. The multicomponent T6SSs are responsible for the translocation of effector molecules into target eukaryotic or prokaryotic cells. The Francisella pathogenicity island encodes a putative T6SS that Francisella novicida requires for intramacrophage growth and virulence during infection of rodents. Here, we present the X-ray crystal structure of the conserved type six secretion component TssL (DotU) from F. novicida. The structure of this protein, which is referred to as Ftn_TssL, revealed an all-α-helical fold that is a unique fusion of two 3-helix bundles. The sequence of Ftn_TssL shows low identity to presumed homologs that are found in most T6SSs. The structure of Ftn_TssL, however, has allowed us to provide bioinformatics evidence that the F. novicida TssL has a fold that is very likely representative for TssL forms from both T6SSs and from the distantly related B subclass of type four secretion systems. A map of sequence conservation on the TssL structure revealed a surface-exposed groove that may represent a functional site on the protein.
PubMed: 22504227
DOI: 10.1016/J.JMB.2012.04.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

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數據於2024-11-06公開中

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