1mvf: Difference between revisions

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[[Image:1mvf.gif|left|200px]]<br />

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

<applet load="1mvf" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1mvf, resolution 1.65Å" />

'''MazE addiction antidote'''<br />

==Overview==

A specific camel VHH (variable domain of dromedary heavy chain antibody), fragment was used to crystallize the intrinsically flexible addiction, antidote MazE. Only 45% of the polypeptide chain is found ordered in the, crystal. The MazE monomer consisting of two beta-hairpins connected by a, short alpha-helix has no hydrophobic core on its own and represents only, one half of a typical protein domain. A complete domain structure is, formed by the association of two chains, creating a hydrophobic core, between two four-stranded beta-sheets. This hydrophobic core consists, exclusively of short aliphatic residues. The folded part of MazE contains, a novel DNA binding motif. A model for DNA binding that is consistent with, the available biochemical data is presented.

A specific camel VHH (variable domain of dromedary heavy chain antibody) fragment was used to crystallize the intrinsically flexible addiction antidote MazE. Only 45% of the polypeptide chain is found ordered in the crystal. The MazE monomer consisting of two beta-hairpins connected by a short alpha-helix has no hydrophobic core on its own and represents only one half of a typical protein domain. A complete domain structure is formed by the association of two chains, creating a hydrophobic core between two four-stranded beta-sheets. This hydrophobic core consists exclusively of short aliphatic residues. The folded part of MazE contains a novel DNA binding motif. A model for DNA binding that is consistent with the available biochemical data is presented.

==About this Structure==

1MVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1MVF OCA].

1MVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVF OCA].

==Reference==

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[[Category: plasmid addiction]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 18 09~~:37:~~28 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:25 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1mvf.gif|left|200px]]<br />
+[[Image:1mvf.gif|left|200px]]<br /><applet load="1mvf" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1mvf" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1mvf, resolution 1.65&Aring;" />
 '''MazE addiction antidote'''<br />
 ==Overview==
-A specific camel VHH (variable domain of dromedary heavy chain antibody), fragment was used to crystallize the intrinsically flexible addiction, antidote MazE. Only 45% of the polypeptide chain is found ordered in the, crystal. The MazE monomer consisting of two beta-hairpins connected by a, short alpha-helix has no hydrophobic core on its own and represents only, one half of a typical protein domain. A complete domain structure is, formed by the association of two chains, creating a hydrophobic core, between two four-stranded beta-sheets. This hydrophobic core consists, exclusively of short aliphatic residues. The folded part of MazE contains, a novel DNA binding motif. A model for DNA binding that is consistent with, the available biochemical data is presented.
+A specific camel VHH (variable domain of dromedary heavy chain antibody) fragment was used to crystallize the intrinsically flexible addiction antidote MazE. Only 45% of the polypeptide chain is found ordered in the crystal. The MazE monomer consisting of two beta-hairpins connected by a short alpha-helix has no hydrophobic core on its own and represents only one half of a typical protein domain. A complete domain structure is formed by the association of two chains, creating a hydrophobic core between two four-stranded beta-sheets. This hydrophobic core consists exclusively of short aliphatic residues. The folded part of MazE contains a novel DNA binding motif. A model for DNA binding that is consistent with the available biochemical data is presented.
 ==About this Structure==
-MVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MVF OCA].
+MVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVF OCA].
 ==Reference==
@@ Line 27: / Line 26: @@
 [[Category: plasmid addiction]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:37:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:25 2008''