1cma: Difference between revisions
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[[Image:1cma.jpg|left|200px]] | [[Image:1cma.jpg|left|200px]] | ||
'''MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE''' | {{Structure | ||
|PDB= 1cma |SIZE=350|CAPTION= <scene name='initialview01'>1cma</scene>, resolution 2.800Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CMA is a [ | 1CMA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMA OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1406951 1406951] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:26:09 2008'' | ||
Revision as of 08:26, 20 March 2008
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| 1cma, resolution 2.800Å | |||||||||||||
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| Ligands: | SAM | ||||||||||||
| 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 Thu Mar 20 10:26:09 2008
