CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.160 | Porin |
|
2.40.160.20 |
Domain Context
CATH Clusters
| Superfamily | 2.40.160.20 |
| Functional Family | Lipid A palmitoyltransferase PagP |
Enzyme Information
| 2.3.1.251 |
Lipid IV(A) palmitoyltransferase.
based on mapping to UniProt P37001
(1) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A. (2) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid II(A) = 2-acyl-sn-glycero-3-phosphocholine + lipid II(B). (3) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IV(A) = 2-acyl-sn-glycero-3-phosphocholine + lipid IV(B).
-!- Isolated from the bacteria Escherichia coli and Salmonella typhimurium. -!- The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. -!- There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. -!- The enzyme also acts on Kdo-(2->4)-Kdo-(2->6)-lipid IV(A).
|
UniProtKB Entries (1)
| P37001 |
PAGP_ECOLI
Escherichia coli K-12
Lipid A palmitoyltransferase PagP
|
PDB Structure
| PDB | 3GP6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler.
Structure
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