1cma: Difference between revisions
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|PDB= 1cma |SIZE=350|CAPTION= <scene name='initialview01'>1cma</scene>, resolution 2.800Å | |PDB= 1cma |SIZE=350|CAPTION= <scene name='initialview01'>1cma</scene>, resolution 2.800Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cma OCA], [http://www.ebi.ac.uk/pdbsum/1cma PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cma RCSB]</span> | |||
}} | }} | ||
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[[Category: Phillips, S E.V.]] | [[Category: Phillips, S E.V.]] | ||
[[Category: Somers, W S.]] | [[Category: Somers, W S.]] | ||
[[Category: double helix]] | [[Category: double helix]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:33 2008'' | ||
Revision as of 19:24, 30 March 2008
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| , resolution 2.800Å | |||||||
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| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE
OverviewOverview
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 StructureAbout this Structure
1CMA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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