1cma
From Proteopedia
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'''MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE''' | '''MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE''' | ||
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[[Category: Phillips, S E.V.]] | [[Category: Phillips, S E.V.]] | ||
[[Category: Somers, W S.]] | [[Category: Somers, W S.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:53:10 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:53, 2 May 2008
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| 1cma, resolution 2.80Å () | |||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
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. 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 Fri May 2 12:53:10 2008


