1cma: Difference between revisions

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

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

caption="1cma, resolution 2.800Å" />

'''MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE'''<br />

==Overview==

The crystal structure of the met repressor-operator complex shows two, dimeric repressor molecules bound to adjacent sites 8 base pairs apart on, an 18-base-pair DNA fragment. Sequence specificity is achieved by, insertion of double-stranded antiparallel protein beta-ribbons into the, major groove of B-form DNA, with direct hydrogen-bonding between, amino-acid side chains and the base pairs. The repressor also recognizes, sequence-dependent distortion or flexibility of the operator phosphate, backbone, conferring specificity even for inaccessible base pairs.

The crystal structure of the met repressor-operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein beta-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognizes sequence-dependent distortion or flexibility of the operator phosphate backbone, conferring specificity even for inaccessible base pairs.

==About this Structure==

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

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

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Phillips, S.E.V.]]

[[Category: Phillips, S E.V.]]

[[Category: Somers, W.S.]]

[[Category: Somers, W S.]]

[[Category: SAM]]

[[Category: double helix]]

[[Category: protein-dna complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 12:34:~~40 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:33 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1cma.jpg|left|200px]]<br /><applet load="1cma" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cma.jpg|left|200px]]<br /><applet load="1cma" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cma, resolution 2.800&Aring;" />
 '''MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE'''<br />
 ==Overview==
-The crystal structure of the met repressor-operator complex shows two, dimeric repressor molecules bound to adjacent sites 8 base pairs apart on, an 18-base-pair DNA fragment. Sequence specificity is achieved by, insertion of double-stranded antiparallel protein beta-ribbons into the, major groove of B-form DNA, with direct hydrogen-bonding between, amino-acid side chains and the base pairs. The repressor also recognizes, sequence-dependent distortion or flexibility of the operator phosphate, backbone, conferring specificity even for inaccessible base pairs.
+The crystal structure of the met repressor-operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein beta-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognizes sequence-dependent distortion or flexibility of the operator phosphate backbone, conferring specificity even for inaccessible base pairs.
 ==About this Structure==
-CMA 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 SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CMA OCA].
+CMA 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=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMA OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Phillips, S.E.V.]]
+[[Category: Phillips, S E.V.]]
-[[Category: Somers, W.S.]]
+[[Category: Somers, W S.]]
 [[Category: SAM]]
 [[Category: double helix]]
 [[Category: protein-dna complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:34:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:33 2008''