2cgp

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|PDB= 2cgp |SIZE=350|CAPTION= <scene name='initialview01'>2cgp</scene>, resolution 2.200&Aring;
|PDB= 2cgp |SIZE=350|CAPTION= <scene name='initialview01'>2cgp</scene>, resolution 2.200&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'>CMP</scene>
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|LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3&#39;,5&#39;-CYCLIC-MONOPHOSPHATE'>CMP</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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[[Category: dna-binding]]
[[Category: dna-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:15:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:52:10 2008''

Revision as of 12:52, 23 March 2008

Image:2cgp.gif


PDB ID 2cgp

Drag the structure with the mouse to rotate
, resolution 2.200Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE


Overview

The 2.2 A resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with cAMP and a 46-bp DNA fragment reveals a second cAMP molecule bound to each protein monomer. The second cAMP is in the syn conformation and is located on the DNA binding domain interacting with the helix-turn-helix, a beta-hairpin from the regulatory domain and the DNA (via water molecules). The presence of this second cAMP site resolves the apparent discrepancy between the NMR and x-ray data on the conformation of cAMP, and explains the cAMP concentration-dependent behaviors of the protein. In addition, this site's close proximity to mutations affecting transcriptional activation and its water-mediated interactions with a DNA recognition residue (E181) and DNA raise the possibility that this site has biological relevance.

About this Structure

2CGP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer., Passner JM, Steitz TA, Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2843-7. PMID:9096308

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