2cgp: Difference between revisions
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=" | [[Image:2cgp.gif|left|200px]]<br /><applet load="2cgp" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2cgp, resolution 2.200Å" /> | caption="2cgp, resolution 2.200Å" /> | ||
'''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 | 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:// | 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 | [[Category: Passner, J M.]] | ||
[[Category: Steitz, T | [[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:// | ''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
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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
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