1chn: Difference between revisions

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[[Image:1chn.jpg|left|200px]]<br /><applet load="1chn" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1chn.jpg|left|200px]]<br /><applet load="1chn" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1chn, resolution 1.76Å" />

'''MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE'''<br />

==Overview==

The three-dimensional crystal structure of the bacterial chemotaxis, protein CheY with the essential Mg2+ cation bound to the active site, reveals large conformational changes caused by the metal binding., Displacements of up to 10 A are observed in several residues at the N, terminus of alpha-helix 4 and in the preceding loop. One turn of this, helix unwinds, and an Asn residue that was located inside the helix, becomes the new N-cap. This supports the important role that N or C-cap, residues play in alpha-helix stability. In addition the preceding, beta-strand becomes elongated and a new beta-turn appears. The final, effect is a significant modification of the surface relief of the protein, in a region previously indicated, by genetic analysis, to be essential for, CheY function. It is suggested that binding of a divalent cation to CheY, could play a significant part in CheY activation and consequently in, signal transduction in prokaryotes.

The three-dimensional crystal structure of the bacterial chemotaxis protein CheY with the essential Mg2+ cation bound to the active site reveals large conformational changes caused by the metal binding. Displacements of up to 10 A are observed in several residues at the N terminus of alpha-helix 4 and in the preceding loop. One turn of this helix unwinds, and an Asn residue that was located inside the helix becomes the new N-cap. This supports the important role that N or C-cap residues play in alpha-helix stability. In addition the preceding beta-strand becomes elongated and a new beta-turn appears. The final effect is a significant modification of the surface relief of the protein in a region previously indicated, by genetic analysis, to be essential for CheY function. It is suggested that binding of a divalent cation to CheY could play a significant part in CheY activation and consequently in signal transduction in prokaryotes.

==About this Structure==

1CHN 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 MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CHN OCA].

1CHN 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=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHN OCA].

==Reference==

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[[Category: signal transduction protein]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:10 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1chn.jpg|left|200px]]<br /><applet load="1chn" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1chn.jpg|left|200px]]<br /><applet load="1chn" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1chn, resolution 1.76&Aring;" />
 '''MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE'''<br />
 ==Overview==
-The three-dimensional crystal structure of the bacterial chemotaxis, protein CheY with the essential Mg2+ cation bound to the active site, reveals large conformational changes caused by the metal binding., Displacements of up to 10 A are observed in several residues at the N, terminus of alpha-helix 4 and in the preceding loop. One turn of this, helix unwinds, and an Asn residue that was located inside the helix, becomes the new N-cap. This supports the important role that N or C-cap, residues play in alpha-helix stability. In addition the preceding, beta-strand becomes elongated and a new beta-turn appears. The final, effect is a significant modification of the surface relief of the protein, in a region previously indicated, by genetic analysis, to be essential for, CheY function. It is suggested that binding of a divalent cation to CheY, could play a significant part in CheY activation and consequently in, signal transduction in prokaryotes.
+The three-dimensional crystal structure of the bacterial chemotaxis protein CheY with the essential Mg2+ cation bound to the active site reveals large conformational changes caused by the metal binding. Displacements of up to 10 A are observed in several residues at the N terminus of alpha-helix 4 and in the preceding loop. One turn of this helix unwinds, and an Asn residue that was located inside the helix becomes the new N-cap. This supports the important role that N or C-cap residues play in alpha-helix stability. In addition the preceding beta-strand becomes elongated and a new beta-turn appears. The final effect is a significant modification of the surface relief of the protein in a region previously indicated, by genetic analysis, to be essential for CheY function. It is suggested that binding of a divalent cation to CheY could play a significant part in CheY activation and consequently in signal transduction in prokaryotes.
 ==About this Structure==
-CHN 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 MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CHN OCA].
+CHN 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=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHN OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: signal transduction protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:27:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:10 2008''