This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1cma

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1cma" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cma, resolution 2.800&Aring;" /> '''MET REPRESSOR/DNA C...)
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;" />
caption="1cma, resolution 2.800&Aring;" />
'''MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE'''<br />
'''MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE'''<br />
==Overview==
==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==
==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==
==Reference==
Line 13: Line 13:
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Phillips, S.E.V.]]
+
[[Category: Phillips, S E.V.]]
-
[[Category: Somers, W.S.]]
+
[[Category: Somers, W S.]]
[[Category: SAM]]
[[Category: SAM]]
[[Category: double helix]]
[[Category: double helix]]
[[Category: protein-dna complex]]
[[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''

Revision as of 10:07, 21 February 2008


1cma, resolution 2.800Å

Drag the structure with the mouse to rotate

MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE

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.

About this Structure

1CMA is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands., Somers WS, Phillips SE, Nature. 1992 Oct 1;359(6394):387-93. PMID:1406951

Page seeded by OCA on Thu Feb 21 12:07:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools