4ACL
3D Structure of DotU from Francisella novicida
Summary for 4ACL
| Entry DOI | 10.2210/pdb4acl/pdb |
| Related | 4ACK |
| Descriptor | TSSL, SODIUM ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | protein transport, t6ss, microbial surface structures, membrane protein, virulence factor |
| Biological source | FRANCISELLA NOVICIDA |
| Total number of polymer chains | 2 |
| Total formula weight | 51127.71 |
| Authors | Robb, C.S.,Nano, F.E.,Boraston, A.B. (deposition date: 2011-12-16, release date: 2012-04-25, Last modification date: 2024-05-08) |
| Primary citation | Robb, 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: 22504227DOI: 10.1016/J.JMB.2012.04.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
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