ArticleActa crystallographica. Section D, Biological crystallography2011
The structure of Serratia marcescens Lip, a membrane-bound component of the type VI secretion system.
Article in Acta crystallographica. Section D, Biological crystallography, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Global identification of Chromobacterium violaceum T6SS effectors reveals an Rhs antibacterial toxin featuring FIX and ADP-ribosyltransferase domains.The Journal of biological chemistry · 2026Article
- First crystal structure of the DUF2436 domain of virulence proteins from Porphyromonas gingivalis.Acta crystallographica. Section F, Structural biology communications · 2024Article
- The accessory protein TagV is required for full Type VI secretion system activity in Serratia marcescens.Molecular microbiology · 2023Article
- Structure and Activity of the Type VI Secretion System.Microbiology spectrum · 2019Review
- Article
- Dual Role for DsbA in Attacking and Targeted Bacterial Cells during Type VI Secretion System-Mediated Competition.Cell reports · 2018Article
- TheFrontiers in cellular and infection microbiology · 2018Review
- Type VI secretion system: secretion by a contractile nanomachine.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Intraspecies Competition in Serratia marcescens Is Mediated by Type VI-Secreted Rhs Effectors and a Conserved Effector-Associated Accessory Protein.Journal of bacteriology · 2015Article
- Production, crystallization and X-ray diffraction analysis of a complex between a fragment of the TssM T6SS protein and a camelid nanobody.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Biochemical analysis of TssK, a core component of the bacterial Type VI secretion system, reveals distinct oligomeric states of TssK and identifies a TssK-TssFG subcomplex.The Biochemical journal · 2014Article
- Structure of Pseudomonas aeruginosa inosine 5'-monophosphate dehydrogenase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Mutation of crp mediates Serratia marcescens serralysin and global secreted protein production.Research in microbiology · 2013Article
- Dissection of the TssB-TssC interface during type VI secretion sheath complex formation.PloS one · 2013Article
- The AEROPATH project targeting Pseudomonas aeruginosa: crystallographic studies for assessment of potential targets in early-stage drug discovery.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Structural characterization and oligomerization of the TssL protein, a component shared by bacterial type VI and type IVb secretion systems.The Journal of biological chemistry · 2012Article
- Structural biology of type VI secretion systems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Structure and regulation of the type VI secretion system.Annual review of microbiology · 2012Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Lip is a membrane-bound lipoprotein and a core component of the type VI secretion system found in Gram-negative bacteria. The structure of a Lip construct (residues 29-176) from Serratia marcescens (SmLip) has been determined at 1.92 Å resolution. Experimental phases were derived using a single-wavelength anomalous dispersion approach on a sample cocrystallized with iodide. The membrane localization of the native protein was confirmed. The structure is that of the globular domain lacking only the lipoprotein signal peptide and the lipidated N-terminus of the mature protein. The protein fold is dominated by an eight-stranded β-sandwich and identifies SmLip as a new member of the transthyretin family of proteins. Transthyretin and the only other member of the family fold, 5-hydroxyisourate hydrolase, form homotetramers important for their function. The asymmetric unit of SmLip is a tetramer with 222 symmetry, but the assembly is distinct from that previously noted for the transthyretin protein family. However, structural comparisons and bacterial two-hybrid data suggest that the SmLip tetramer is not relevant to its role as a core component of the type VI secretion system, but rather reflects a propensity for SmLip to participate in protein-protein interactions. A relatively low level of sequence conservation amongst Lip homologues is noted and is restricted to parts of the structure that might be involved in interactions with physiological partners.
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