1lb2: Difference between revisions
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|PDB= 1lb2 |SIZE=350|CAPTION= <scene name='initialview01'>1lb2</scene>, resolution 3.1Å | |PDB= 1lb2 |SIZE=350|CAPTION= <scene name='initialview01'>1lb2</scene>, resolution 3.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'>CMP</scene> | |LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <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> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lb2 OCA], [http://www.ebi.ac.uk/pdbsum/1lb2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lb2 RCSB]</span> | |||
}} | }} | ||
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[[Category: Parkinson, G.]] | [[Category: Parkinson, G.]] | ||
[[Category: Yang, H.]] | [[Category: Yang, H.]] | ||
[[Category: gene-regulatory]] | [[Category: gene-regulatory]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:00:32 2008'' | ||
Revision as of 19:00, 30 March 2008
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| 1lb2, resolution 3.1Å | |||||||||||||
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| Ligands: | CMP, DA, DC, DG, DT | ||||||||||||
| Activity: | DNA-directed RNA polymerase, with EC number 2.7.7.6 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structure of the E. coli alpha C-terminal domain of RNA polymerase in complex with CAP and DNA
Overview
The Escherichia coli catabolite activator protein (CAP) activates transcription at P(lac), P(gal), and other promoters through interactions with the RNA polymerase alpha subunit carboxyl-terminal domain (alphaCTD). We determined the crystal structure of the CAP-alphaCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with alphaCTD, and alphaCTD makes direct protein-DNA interactions with the DNA segment adjacent to the DNA site for CAP. There are no large-scale conformational changes in CAP and alphaCTD, and the interface between CAP and alphaCTD is small. These findings are consistent with the proposal that activation involves a simple "recruitment" mechanism.
About this Structure
1LB2 is a Protein complex structure of sequences from Escherichia coli. The following page contains interesting information on the relation of 1LB2 with [Catabolite Activator Protein]. Full crystallographic information is available from OCA.
Reference
Structural basis of transcription activation: the CAP-alpha CTD-DNA complex., Benoff B, Yang H, Lawson CL, Parkinson G, Liu J, Blatter E, Ebright YW, Berman HM, Ebright RH, Science. 2002 Aug 30;297(5586):1562-6. PMID:12202833
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