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J Biol Chem, Vol. 273, Issue 28, 17604-17609, July 10, 1998

Crystal Structure and Mutational Analysis of the Escherichia coli Putrescine Receptor
STRUCTURAL BASIS FOR SUBSTRATE SPECIFICITY

Dmitry G. Vassylyev, Hideyuki Tomitori^¶, Keiko Kashiwagi^¶, Kosuke Morikawa, and Kazuei Igarashi^¶

From the  Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka, 565-0874 and ^¶ Faculty of Pharmaceutical Sciences, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan

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-Å resolution. The PotF molecule has dimensions of 54 × 42 × 30 Å 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.

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