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1cma
From Proteopedia
| 1cma, resolution 2.80Å () | |||||||||
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| Ligands: | |||||||||
| Domains: | Met_repressor_MetJ | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1CMA is a 4 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Somers WS, Phillips SE. Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands. Nature. 1992 Oct 1;359(6394):387-93. PMID:1406951 doi:10.1038/359387a0
Page seeded by OCA on Mon Feb 16 19:57:51 2009
