1t98: Difference between revisions

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[[Image:1t98.gif|left|200px]]<br /><applet load="1t98" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1t98.gif|left|200px]]<br /><applet load="1t98" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1t98, resolution 2.90Å" />

'''Crystal Structure of MukF(1-287)'''<br />

==Overview==

The Escherichia coli MukB, MukE, and MukF proteins form a bacterial, condensin (MukBEF) that contributes to chromosome management by compacting, DNA. MukB is an ATPase and DNA-binding protein of the SMC superfamily;, however, the structure and function of non-SMC components, such as MukF, have been less forthcoming. Here, we report the crystal structure of the, N-terminal 287 amino acids of MukF at 2.9 A resolution. This region folds, into a winged-helix domain and an extended coiled-coil domain that, self-associate to form a stable, doubly domain-swapped dimer. Protein, dissection and affinity purification data demonstrate that the region of, MukF C-terminal to this fragment binds to MukE and MukB. Our findings, together with sequence analyses, indicate that MukF is a kleisin subunit, for E. coli condensin and suggest a means by which it may organize the, MukBEF assembly.

The Escherichia coli MukB, MukE, and MukF proteins form a bacterial condensin (MukBEF) that contributes to chromosome management by compacting DNA. MukB is an ATPase and DNA-binding protein of the SMC superfamily; however, the structure and function of non-SMC components, such as MukF, have been less forthcoming. Here, we report the crystal structure of the N-terminal 287 amino acids of MukF at 2.9 A resolution. This region folds into a winged-helix domain and an extended coiled-coil domain that self-associate to form a stable, doubly domain-swapped dimer. Protein dissection and affinity purification data demonstrate that the region of MukF C-terminal to this fragment binds to MukE and MukB. Our findings, together with sequence analyses, indicate that MukF is a kleisin subunit for E. coli condensin and suggest a means by which it may organize the MukBEF assembly.

==About this Structure==

1T98 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=1T98 OCA].

1T98 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=1T98 OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Berger, J.M.]]

[[Category: Berger, J M.]]

[[Category: Fennell-Fezzie, R.]]

[[Category: coiled coil]]

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[[Category: winged helix]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:14 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1t98.gif|left|200px]]<br /><applet load="1t98" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1t98.gif|left|200px]]<br /><applet load="1t98" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1t98, resolution 2.90&Aring;" />
 '''Crystal Structure of MukF(1-287)'''<br />
 ==Overview==
-The Escherichia coli MukB, MukE, and MukF proteins form a bacterial, condensin (MukBEF) that contributes to chromosome management by compacting, DNA. MukB is an ATPase and DNA-binding protein of the SMC superfamily;, however, the structure and function of non-SMC components, such as MukF, have been less forthcoming. Here, we report the crystal structure of the, N-terminal 287 amino acids of MukF at 2.9 A resolution. This region folds, into a winged-helix domain and an extended coiled-coil domain that, self-associate to form a stable, doubly domain-swapped dimer. Protein, dissection and affinity purification data demonstrate that the region of, MukF C-terminal to this fragment binds to MukE and MukB. Our findings, together with sequence analyses, indicate that MukF is a kleisin subunit, for E. coli condensin and suggest a means by which it may organize the, MukBEF assembly.
+The Escherichia coli MukB, MukE, and MukF proteins form a bacterial condensin (MukBEF) that contributes to chromosome management by compacting DNA. MukB is an ATPase and DNA-binding protein of the SMC superfamily; however, the structure and function of non-SMC components, such as MukF, have been less forthcoming. Here, we report the crystal structure of the N-terminal 287 amino acids of MukF at 2.9 A resolution. This region folds into a winged-helix domain and an extended coiled-coil domain that self-associate to form a stable, doubly domain-swapped dimer. Protein dissection and affinity purification data demonstrate that the region of MukF C-terminal to this fragment binds to MukE and MukB. Our findings, together with sequence analyses, indicate that MukF is a kleisin subunit for E. coli condensin and suggest a means by which it may organize the MukBEF assembly.
 ==About this Structure==
-T98 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=1T98 OCA].
+T98 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=1T98 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Berger, J.M.]]
+[[Category: Berger, J M.]]
 [[Category: Fennell-Fezzie, R.]]
 [[Category: coiled coil]]
@@ Line 21: / Line 21: @@
 [[Category: winged helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:05:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:14 2008''