2f1n: Difference between revisions

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[[Image:2f1n.gif|left|200px]]<br /><applet load="2f1n" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2f1n.gif|left|200px]]<br /><applet load="2f1n" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2f1n, resolution 1.73Å" />

'''Structure of CdtB, the biologically active subunit of Cytolethal Distending Toxin'''<br />

==Overview==

Cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis, in eukaryotic cells, which are mediated by the DNA-damaging CdtB subunit., Here we report the first x-ray structure of an isolated CdtB subunit, (Escherichia coli-II CdtB, EcCdtB). In conjunction with previous, structural and biochemical observations, active site structural, comparisons between free and holotoxin-assembled CdtBs suggested that CDT, intoxication is contingent upon holotoxin disassembly. Solution NMR, structural and 15N relaxation studies of free EcCdtB revealed disorder in, the interface with the CdtA and CdtC subunits (residues Gly233-Asp242)., Residues Leu186-Thr209 of EcCdtB, which encompasses tandem arginine, residues essential for nuclear translocation and intoxication, were also, disordered in solution. In stark contrast, nearly identical well defined, alpha-helix and beta-strand secondary structures were observed in this, region of the free and holotoxin CdtB crystallographic models, suggesting, that distinct changes in structural ordering characterize subunit, disassembly and nuclear localization factor binding functions.

Cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis in eukaryotic cells, which are mediated by the DNA-damaging CdtB subunit. Here we report the first x-ray structure of an isolated CdtB subunit (Escherichia coli-II CdtB, EcCdtB). In conjunction with previous structural and biochemical observations, active site structural comparisons between free and holotoxin-assembled CdtBs suggested that CDT intoxication is contingent upon holotoxin disassembly. Solution NMR structural and 15N relaxation studies of free EcCdtB revealed disorder in the interface with the CdtA and CdtC subunits (residues Gly233-Asp242). Residues Leu186-Thr209 of EcCdtB, which encompasses tandem arginine residues essential for nuclear translocation and intoxication, were also disordered in solution. In stark contrast, nearly identical well defined alpha-helix and beta-strand secondary structures were observed in this region of the free and holotoxin CdtB crystallographic models, suggesting that distinct changes in structural ordering characterize subunit disassembly and nuclear localization factor binding functions.

==About this Structure==

2F1N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2F1N OCA].

2F1N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1N OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Dreyfus, L.A.]]

[[Category: Dreyfus, L A.]]

[[Category: Hontz, J.S.]]

[[Category: Hontz, J S.]]

[[Category: Yoder, M.D.]]

[[Category: Yoder, M D.]]

[[Category: cdt]]

[[Category: cytolethal distending toxin]]

[[Category: dnase i]]

[[Category: e.coli]]

[[Category: e coli]]

[[Category: microbatch]]

[[Category: toxin]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 10:18:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:52 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2f1n.gif|left|200px]]<br /><applet load="2f1n" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2f1n.gif|left|200px]]<br /><applet load="2f1n" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2f1n, resolution 1.73&Aring;" />
 '''Structure of CdtB, the biologically active subunit of Cytolethal Distending Toxin'''<br />
 ==Overview==
-Cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis, in eukaryotic cells, which are mediated by the DNA-damaging CdtB subunit., Here we report the first x-ray structure of an isolated CdtB subunit, (Escherichia coli-II CdtB, EcCdtB). In conjunction with previous, structural and biochemical observations, active site structural, comparisons between free and holotoxin-assembled CdtBs suggested that CDT, intoxication is contingent upon holotoxin disassembly. Solution NMR, structural and 15N relaxation studies of free EcCdtB revealed disorder in, the interface with the CdtA and CdtC subunits (residues Gly233-Asp242)., Residues Leu186-Thr209 of EcCdtB, which encompasses tandem arginine, residues essential for nuclear translocation and intoxication, were also, disordered in solution. In stark contrast, nearly identical well defined, alpha-helix and beta-strand secondary structures were observed in this, region of the free and holotoxin CdtB crystallographic models, suggesting, that distinct changes in structural ordering characterize subunit, disassembly and nuclear localization factor binding functions.
+Cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis in eukaryotic cells, which are mediated by the DNA-damaging CdtB subunit. Here we report the first x-ray structure of an isolated CdtB subunit (Escherichia coli-II CdtB, EcCdtB). In conjunction with previous structural and biochemical observations, active site structural comparisons between free and holotoxin-assembled CdtBs suggested that CDT intoxication is contingent upon holotoxin disassembly. Solution NMR structural and 15N relaxation studies of free EcCdtB revealed disorder in the interface with the CdtA and CdtC subunits (residues Gly233-Asp242). Residues Leu186-Thr209 of EcCdtB, which encompasses tandem arginine residues essential for nuclear translocation and intoxication, were also disordered in solution. In stark contrast, nearly identical well defined alpha-helix and beta-strand secondary structures were observed in this region of the free and holotoxin CdtB crystallographic models, suggesting that distinct changes in structural ordering characterize subunit disassembly and nuclear localization factor binding functions.
 ==About this Structure==
-F1N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F1N OCA].
+F1N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1N OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Dreyfus, L.A.]]
+[[Category: Dreyfus, L A.]]
-[[Category: Hontz, J.S.]]
+[[Category: Hontz, J S.]]
-[[Category: Yoder, M.D.]]
+[[Category: Yoder, M D.]]
 [[Category: cdt]]
 [[Category: cytolethal distending toxin]]
 [[Category: dnase i]]
-[[Category: e.coli]]
+[[Category: e coli]]
 [[Category: microbatch]]
 [[Category: toxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:18:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:52 2008''