1g6n
From Proteopedia
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'''2.1 ANGSTROM STRUCTURE OF CAP-CAMP''' | '''2.1 ANGSTROM STRUCTURE OF CAP-CAMP''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 | + | 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 and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gap 1gap]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6N OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Schultz, S C.]] | [[Category: Schultz, S C.]] | ||
[[Category: Steitz, T A.]] | [[Category: Steitz, T A.]] | ||
| - | [[Category: | + | [[Category: Allostery]] |
| - | [[Category: | + | [[Category: Camp]] |
| - | [[Category: | + | [[Category: Cyclic amp]] |
| - | + | [[Category: Transcription]] | |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:12:18 2008'' | |
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Revision as of 14:12, 2 May 2008
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 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 Page seeded by OCA on Fri May 2 17:12:18 2008
