1g6n
From Proteopedia
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| - | [[Image:1g6n.jpg|left|200px]] | + | [[Image:1g6n.jpg|left|200px]] |
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| - | '''2.1 ANGSTROM STRUCTURE OF CAP-CAMP''' | + | {{Structure |
| + | |PDB= 1g6n |SIZE=350|CAPTION= <scene name='initialview01'>1g6n</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'>CMP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''2.1 ANGSTROM STRUCTURE OF CAP-CAMP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G6N is a [ | + | 1G6N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries 3GAP and 1GAP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6N OCA]. |
==Reference== | ==Reference== | ||
| - | Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution., Passner JM, Schultz SC, Steitz TA, J Mol Biol. 2000 Dec 15;304(5):847-59. PMID:[http:// | + | Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution., Passner JM, Schultz SC, Steitz TA, J Mol Biol. 2000 Dec 15;304(5):847-59. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11124031 11124031] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''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 11:18:54 2008'' |
Revision as of 09:18, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
2.1 ANGSTROM STRUCTURE OF CAP-CAMP
Overview
After an allosteric transition produced by the binding of cyclic AMP (cAMP), the Escherichia coli catabolite gene activator protein (CAP) binds DNA specifically and activates transcription. The three-dimensional crystal structure of the CAP-cAMP complex has been refined at 2.1 A resolution, thus enabling a better evaluation of the structural basis for CAP phenotypes, the interactions of cAMP with CAP and the roles played by water structure. A review of mutational analysis of CAP together with the additional structural information presented here suggests a possible mechanism for the cAMP-induced allostery required for DNA binding and transcriptional activation. We hypothesize that cAMP binding may reorient the coiled-coil C-helices, which provide most of the dimer interface, thereby altering the relative positions of the DNA-binding domains of the CAP dimer. Additionally, cAMP binding may cause a further rearrangement of the DNA-binding and cAMP-binding domains of CAP via a flap consisting of beta-strands 4 and 5 which lies over the cAMP.
About this Structure
1G6N is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entries 3GAP and 1GAP. Full crystallographic information is available from OCA.
Reference
Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution., Passner JM, Schultz SC, Steitz TA, J Mol Biol. 2000 Dec 15;304(5):847-59. PMID:11124031
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