1by3: Difference between revisions

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New page: left|200px<br /><applet load="1by3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1by3, resolution 2.74Å" /> '''FHUA FROM E. COLI'''...
 
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[[Image:1by3.jpg|left|200px]]<br /><applet load="1by3" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1by3.jpg|left|200px]]<br /><applet load="1by3" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1by3, resolution 2.74&Aring;" />
caption="1by3, resolution 2.74&Aring;" />
'''FHUA FROM E. COLI'''<br />
'''FHUA FROM E. COLI'''<br />


==Overview==
==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.
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.


==About this Structure==
==About this Structure==
1BY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with OES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BY3 OCA].  
1BY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=OES:'>OES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY3 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Koebnik, R.]]
[[Category: Koebnik, R.]]
[[Category: Locher, K.P.]]
[[Category: Locher, K P.]]
[[Category: Mitschler, A.]]
[[Category: Mitschler, A.]]
[[Category: Moras, D.]]
[[Category: Moras, D.]]
[[Category: Moulinier, L.]]
[[Category: Moulinier, L.]]
[[Category: Rees, B.]]
[[Category: Rees, B.]]
[[Category: Rosenbusch, J.P.]]
[[Category: Rosenbusch, J P.]]
[[Category: OES]]
[[Category: OES]]
[[Category: fhua]]
[[Category: fhua]]
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[[Category: membrane protein]]
[[Category: membrane protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:00:59 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:21 2008''