1by5: Difference between revisions

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~~'''~~FHUA FROM E. COLI, WITH ITS LIGAND FERRICHROME~~'''~~

===FHUA FROM E. COLI, WITH ITS LIGAND FERRICHROME===

~~==Overview==~~

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~~FhuA protein facilitates ligand~~-~~gated transport of ferrichrome~~-~~bound iron across Escherichia coli outer membranes. X-ray analysis at 2.7 A resolution reveals two distinct conformations in the presence and absence of ferrichrome.~~ The ~~monomeric protein consists of a hollow~~, ~~22-stranded~~, ~~antiparallel beta barrel~~ (~~residues 160-714~~), ~~which~~ is ~~obstructed by a plug (residues 19-159). The binding site of ferrichrome, an aromatic pocket near~~ the ~~cell surface, undergoes minor changes upon association with the ligand~~. These are propagated and amplified across the plug, eventually resulting in substantially different protein conformations at the periplasmic face. Our findings reveal the mechanism of signal transmission and suggest how the energy-~~transducing TonB complex senses ligand binding.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9865695}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9865695 is the PubMed ID number.

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==About this Structure==

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[[Category: Ligand-gated]]

[[Category: Membrane protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:06:19 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:54:16 2008''

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-[[Image:1by5.jpg|left|200px]]
+{{Seed}}
+[[Image:1by5.png|left|200px]]
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 {{STRUCTURE_1by5|  PDB=1by5  |  SCENE=  }}
-'''FHUA FROM E. COLI, WITH ITS LIGAND FERRICHROME'''
+===FHUA FROM E. COLI, WITH ITS LIGAND FERRICHROME===
-==Overview==
+<!--
-FhuA protein facilitates ligand-gated transport of ferrichrome-bound iron across Escherichia coli outer membranes. X-ray analysis at 2.7 A resolution reveals two distinct conformations in the presence and absence of ferrichrome. The monomeric protein consists of a hollow, 22-stranded, antiparallel beta barrel (residues 160-714), which is obstructed by a plug (residues 19-159). The binding site of ferrichrome, an aromatic pocket near the cell surface, undergoes minor changes upon association with the ligand. These are propagated and amplified across the plug, eventually resulting in substantially different protein conformations at the periplasmic face. Our findings reveal the mechanism of signal transmission and suggest how the energy-transducing TonB complex senses ligand binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_9865695}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9865695 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9865695}}
 ==About this Structure==
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 [[Category: Ligand-gated]]
 [[Category: Membrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:06:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:54:16 2008''