2wc2
From Proteopedia
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Revision as of 07:24, 6 May 2009
NMR STRUCTURE OF CATABOLITE ACTIVATOR PROTEIN IN THE UNLIGANDED STATE
Template:ABSTRACT PUBMED 19359484
About this Structure
2WC2 is a 2 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Popovych N, Tzeng SR, Tonelli M, Ebright RH, Kalodimos CG. Structural basis for cAMP-mediated allosteric control of the catabolite activator protein. Proc Natl Acad Sci U S A. 2009 Apr 9. PMID:19359484
Page seeded by OCA on Wed May 6 10:24:41 2009
Categories: Escherichia coli | Kalodimos, C G. | Popovych, N. | Tzeng, S R. | Acetylation | Activator | Allosteric protein | Camp | Camp-binding | Catabolite activator protein | Cyclic nucleotide-binding protein | Dna-binding | Dna-binding protein | Nucleotide-binding | Transcription | Transcription regulation | Transcription regulator | Transctiption factor
