2cgp

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[[Image:2cgp.gif|left|200px]]
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{{STRUCTURE_2cgp| PDB=2cgp | SCENE= }}
{{STRUCTURE_2cgp| PDB=2cgp | SCENE= }}
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'''CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'''
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===CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9096308 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9096308}}
==About this Structure==
==About this Structure==
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[[Category: Camp-binding]]
[[Category: Camp-binding]]
[[Category: Dna-binding]]
[[Category: Dna-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:06:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:40:02 2008''

Revision as of 20:40, 27 July 2008

Image:2cgp.png

Template:STRUCTURE 2cgp

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

Template:ABSTRACT PUBMED 9096308

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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