2cgp: Difference between revisions

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New page: left|200px<br /><applet load="2cgp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cgp, resolution 2.200Å" /> '''CATABOLITE GENE ACT...
 
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[[Image:2cgp.gif|left|200px]]<br /><applet load="2cgp" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2cgp.gif|left|200px]]<br /><applet load="2cgp" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2cgp, resolution 2.200&Aring;" />
caption="2cgp, resolution 2.200&Aring;" />
'''CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'''<br />
'''CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'''<br />


==Overview==
==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.
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==
==About this Structure==
2CGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CMP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CGP OCA].  
2CGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CMP:'>CMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CGP OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Passner, J.M.]]
[[Category: Passner, J M.]]
[[Category: Steitz, T.A.]]
[[Category: Steitz, T A.]]
[[Category: CMP]]
[[Category: CMP]]
[[Category: activator]]
[[Category: activator]]
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[[Category: dna-binding]]
[[Category: dna-binding]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:58:47 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:25 2008''

Revision as of 17:48, 21 February 2008

File:2cgp.gif


2cgp, resolution 2.200Å

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

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 16:48:25 2008

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