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Literature summary for 2.7.8.43 extracted from
- Lipopolysaccharide binding to the periplasmic protein LptA (2017), Protein Sci., 26, 1517-1523 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene lptA, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| I36R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| I36R1/Q148A/K149A | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| I86R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| I86R1/Q148A/K149A | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| L145R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| L45R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| M98R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| N185R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| N185R1/Q148A/K149A | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| Q148A/K149A | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| S110R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| T32R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| V132R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
| V165R1 | site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | possibly one or more LptA proteins bridges the periplasm to form a large, connected protein complex | Escherichia coli | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0ADV1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by cobalt affinity chromatography, dialysis, and ultrafiltration | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | quantitative analysis of binding of LPS by LptA, 1:1 ratio for the LPS:LptA complex, and structure analysis of the LPS binding pocket. The entire LptA protein is affected by LPS binding, the N-terminus unfolds in the presence of LPS | Escherichia coli | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | according to light scattering data, LptA oligomerizes in a concentration-dependent manner. LptA is an average of a trimer in solution, and a considerably higher order oligomerization state (25mers) is predicted at a protein concentration of 0.1 mM | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LptA | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | LptA is a member of the lipopolysaccharide transport protein (Lpt) family | Escherichia coli |
| malfunction | a mutant LptA protein unable to form oligomers has an altered affinity for LPS | Escherichia coli |
| physiological function | LptA functions to transport lipopolysaccharide (LPS) through the periplasm to the outer leaflet of the outer membrane after ABC transporter MsbA flips LPS across the inner membrane. It is hypothesized that LPS binds to LptA to cross the periplasm and that the acyl chains of LPS bind to the central pocket of LptA | Escherichia coli |
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