1poy
From Proteopedia
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| - | [[Image:1poy.jpg|left|200px]] | + | [[Image:1poy.jpg|left|200px]] |
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| - | '''SPERMIDINE/PUTRESCINE-BINDING PROTEIN COMPLEXED WITH SPERMIDINE (DIMER FORM)''' | + | {{Structure |
| + | |PDB= 1poy |SIZE=350|CAPTION= <scene name='initialview01'>1poy</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SPERMIDINE/PUTRESCINE-BINDING PROTEIN COMPLEXED WITH SPERMIDINE (DIMER FORM)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1POY is a [ | + | 1POY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POY OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli., Sugiyama S, Vassylyev DG, Matsushima M, Kashiwagi K, Igarashi K, Morikawa K, J Biol Chem. 1996 Apr 19;271(16):9519-25. PMID:[http:// | + | Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli., Sugiyama S, Vassylyev DG, Matsushima M, Kashiwagi K, Igarashi K, Morikawa K, J Biol Chem. 1996 Apr 19;271(16):9519-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8621624 8621624] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:27:09 2008'' |
Revision as of 11:27, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
SPERMIDINE/PUTRESCINE-BINDING PROTEIN COMPLEXED WITH SPERMIDINE (DIMER FORM)
Overview
PotD protein is a periplasmic binding protein and the primary receptor of the polyamine transport system, which regulates the polyamine content in Escherichia coli. The crystal structure of PotD in complex with spermidine has been solved at 2.5-A resolution. The PotD protein consists of two domains with an alternating beta-alpha-beta topology. The polyamine binding site is in a central cleft lying in the interface between the domains. In the cleft, four acidic residues recognize the three positively charged nitrogen atoms of spermidine, while five aromatic side chains anchor the methylene backbone by van der Waals interactions. The overall fold of PotD is similar to that of other periplasmic binding proteins, and in particular to the maltodextrin-binding protein from E. coli, despite the fact that sequence identity is as low as 20%. The comparison of the PotD structure with the two maltodextrin-binding protein structures, determined in the presence and absence of the substrate, suggests that spermidine binding rearranges the relative orientation of the PotD domains to create a more compact structure.
About this Structure
1POY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli., Sugiyama S, Vassylyev DG, Matsushima M, Kashiwagi K, Igarashi K, Morikawa K, J Biol Chem. 1996 Apr 19;271(16):9519-25. PMID:8621624
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