Joe Granger Methionine Repressor: Escherichia coli
From Proteopedia
| Line 5: | Line 5: | ||
===MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE=== | ===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. }} | + | {{ The Met Repressor Protein is involved with regulating the synthesis of methionine. This protein works to bind the DNA operatiors that activate the transcription of genes that produce methionine. When this protein is bound to DNA, it prevents RNA polymerase 11 from binding and promoting transcription. 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. The <scene name='User:Wally_Novak/Suface_of_the_protein/3'>TextToBeDisplayed</scene> is bound tightly with The DNA operator in the major groove 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== | ||
Revision as of 00:29, 8 November 2012
| |||||||||
| 1cma, resolution 2.80Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | |||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE
{{ The Met Repressor Protein is involved with regulating the synthesis of methionine. This protein works to bind the DNA operatiors that activate the transcription of genes that produce methionine. When this protein is bound to DNA, it prevents RNA polymerase 11 from binding and promoting transcription. 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. The is bound tightly with The DNA operator in the major groove 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 4 chain structure with sequence 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:http://dx.doi.org/10.1038/359387a0
