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2cgp
From Proteopedia
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| - | [[Image:2cgp.gif|left|200px]] | + | [[Image:2cgp.gif|left|200px]] |
| - | + | ||
| - | '''CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE''' | + | {{Structure |
| + | |PDB= 2cgp |SIZE=350|CAPTION= <scene name='initialview01'>2cgp</scene>, resolution 2.200Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'>CMP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CGP is a [ | + | 2CGP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CGP OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9096308 9096308] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dna-binding]] | [[Category: dna-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:15:07 2008'' |
Revision as of 14:15, 20 March 2008
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| , resolution 2.200Å | |||||||
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| 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
Page seeded by OCA on Thu Mar 20 16:15:07 2008
