FhuD: Difference between revisions

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<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

==PERIPLASMIC FERRIC SIDEROPHORE BINDING PROTEIN FHUD COMPLEXED WITH COPROGEN (1esz)==

=='''PERIPLASMIC FERRIC SIDEROPHORE BINDING PROTEIN FHUD COMPLEXED WITH COPROGEN (1esz)'''==

~~Leni Rose~~

==OVERVIEW==

Siderophore-binding proteins can be found in both Gram-positive and Gram-negative bacteria in two divisions: hydroxamates and catecholates. In Escherichia coli. (E. coli) the ATP-binding cassette- type (ABC-type) protein FhuD is a common periplasmic protein which facilitates the transport of a variety of hydoxamate siderophores to the inner membrane-associated proteins FhuB and FhuC. The structure of FhuD is atypical for periplasmic ligand binding protein due to its bilobal mixture of two α/β domains connected by long α-helix.

==PROTEIN STRUCTURE==

FhuD is atypical for periplasmic ligand binding proteins. It is a bilobal kidney bean shape containing two domains which are connected by a 23-residue kinked α-helix. The N-terminal domain twisted fived-stranded parallel β-sheet whereas the C-terminal domain has a mixed five stranded β-sheet; both are surrounded by α-helices. Between the two domains lies the siderophore binding in the shallow pocket. In this pocket, side chain residues are able to hydrogen bond with the accepted siderophore.

~~==PROTEIN STUCTURE==~~

==PROTEIN FUNCTION==

~~<applet load='1esz' size='300' frame='true' align='right' caption='Insert caption here' />~~

[[User:Leni Rose|Leni Rose]] 04:57, 13 March 2010 (IST)

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@@ Line 1: / Line 1: @@
 <table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>
-==PERIPLASMIC FERRIC SIDEROPHORE BINDING PROTEIN FHUD COMPLEXED WITH COPROGEN (1esz)==
+=='''PERIPLASMIC FERRIC SIDEROPHORE BINDING PROTEIN FHUD COMPLEXED WITH COPROGEN (1esz)'''==
-Leni Rose
+<applet load='1esz' size='300' frame='true' align='right' caption='Insert caption here' />
 ==OVERVIEW==
+Siderophore-binding proteins can be found in both Gram-positive and Gram-negative bacteria in two divisions: hydroxamates and catecholates. In Escherichia coli. (E. coli) the ATP-binding cassette- type (ABC-type) protein FhuD is a common periplasmic protein which facilitates the transport of a variety of hydoxamate siderophores to the inner membrane-associated proteins FhuB and FhuC. The structure of FhuD is atypical for periplasmic ligand binding protein due to its bilobal mixture of two α/β domains connected by long α-helix.
+==PROTEIN STRUCTURE==
+FhuD is atypical for periplasmic ligand binding proteins. It is a bilobal kidney bean shape containing two domains which are connected by a 23-residue kinked α-helix. The N-terminal domain twisted fived-stranded parallel β-sheet whereas the C-terminal domain has a mixed five stranded β-sheet; both are surrounded by α-helices. Between the two domains lies the siderophore binding in the shallow pocket. In this pocket, side chain residues are able to hydrogen bond with the accepted siderophore.
-==PROTEIN STUCTURE==
 ==PROTEIN FUNCTION==
-<applet load='1esz' size='300' frame='true' align='right' caption='Insert caption here' />
+[[User:Leni Rose|Leni Rose]] 04:57, 13 March 2010 (IST)