1a99: Difference between revisions
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'''PUTRESCINE RECEPTOR (POTF) FROM E. COLI''' | '''PUTRESCINE RECEPTOR (POTF) FROM E. COLI''' | ||
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[[Category: Tomitori, H.]] | [[Category: Tomitori, H.]] | ||
[[Category: Vassylyev, D G.]] | [[Category: Vassylyev, D G.]] | ||
[[Category: | [[Category: Binding protein]] | ||
[[Category: | [[Category: Transport]] | ||
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Revision as of 10:00, 2 May 2008
PUTRESCINE RECEPTOR (POTF) FROM E. COLI
OverviewOverview
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.
About this StructureAbout this Structure
1A99 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 10:00:36 2008