Structural highlights
Function
[POTF_ECOLI] Required for the activity of the bacterial periplasmic transport system of putrescine. Polyamine binding protein.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
PotF protein is a periplasmic substrate-binding protein of the putrescine transport system in Escherichia coli. We have determined the crystal structure of PotF protein in complex with the substrate at 2.3-A resolution. The PotF molecule has dimensions of 54 x 42 x 30 A and consists of two similar globular domains. The PotF structure is reminiscent of other periplasmic receptors with a highest structural homology to another polyamine-binding protein, PotD. Putrescine is tightly bound in the deep cleft between the two domains of PotF through 12 hydrogen bonds and 36 van der Waals interactions. The comparison of the PotF structure with that of PotD provides the insight into the differences in the specificity between the two proteins. The PotF structure, in combination with the mutational analysis, revealed the residues crucial for putrescine binding (Trp-37, Ser-85, Glu-185, Trp-244, Asp-247, and Asp-278) and the importance of water molecules for putrescine recognition.
Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity.,Vassylyev DG, Tomitori H, Kashiwagi K, Morikawa K, Igarashi K J Biol Chem. 1998 Jul 10;273(28):17604-9. PMID:9651355[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vassylyev DG, Tomitori H, Kashiwagi K, Morikawa K, Igarashi K. Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity. J Biol Chem. 1998 Jul 10;273(28):17604-9. PMID:9651355
