1g6n

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{{STRUCTURE_1g6n| PDB=1g6n | SCENE= }}
{{STRUCTURE_1g6n| PDB=1g6n | SCENE= }}
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'''2.1 ANGSTROM STRUCTURE OF CAP-CAMP'''
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===2.1 ANGSTROM STRUCTURE OF CAP-CAMP===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_11124031}}
==About this Structure==
==About this Structure==
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[[Category: Cyclic amp]]
[[Category: Cyclic amp]]
[[Category: Transcription]]
[[Category: Transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:44:57 2008''

Revision as of 01:45, 1 July 2008

Template:STRUCTURE 1g6n

2.1 ANGSTROM STRUCTURE OF CAP-CAMP

Template:ABSTRACT PUBMED 11124031

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

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