1g6n

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|ACTIVITY=
|ACTIVITY=
|GENE=
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|RELATEDENTRY=[[3gap|3GAP]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6n OCA], [http://www.ebi.ac.uk/pdbsum/1g6n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g6n RCSB]</span>
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[[Category: Schultz, S C.]]
[[Category: Schultz, S C.]]
[[Category: Steitz, T A.]]
[[Category: Steitz, T A.]]
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[[Category: CMP]]
 
[[Category: allostery]]
[[Category: allostery]]
[[Category: camp]]
[[Category: camp]]
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[[Category: transcription]]
[[Category: transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:53:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:37:44 2008''

Revision as of 17:37, 30 March 2008


PDB ID 1g6n

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands:
Related: 3GAP


Resources: FirstGlance, OCA, PDBsum, RCSB
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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