1rl3
From Proteopedia
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| , resolution 2.70Å | |||||||
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| Ligands: | , | ||||||
| Gene: | PRKAR1A (Bos taurus) | ||||||
| Related: | 1RGS, 1NE4, 1NE6
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of cAMP-free R1a subunit of PKA
Overview
In eukaryotes the primary target for cAMP, a ubiquitous second messenger, is cAMP-dependent protein kinase (PKA). Understanding how binding and release of cAMP changes the cAMP binding domains and then triggers long-range allosteric responses is an important challenge. This conformational switching requires structure solutions of cAMP binding domains in cAMP-bound and cAMP-free states. We describe for the first time a crystal structure of the cAMP binding domains of PKA type Ialpha regulatory subunit where site A is occupied by cGMP and site B is unoccupied. The structure reveals that the carboxyl terminus of domain B serves as a hydrophobic cap, locking the cyclic nucleotide via its adenine ring into the beta-barrel. In the absence of cAMP, the "cap" is released via an extension of the C-terminal helix. This simple hinge mechanism for binding and release of cAMP also provides a mechanism for allosteric communication between sites A and B.
About this Structure
1RL3 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
RIalpha subunit of PKA: a cAMP-free structure reveals a hydrophobic capping mechanism for docking cAMP into site B., Wu J, Brown S, Xuong NH, Taylor SS, Structure. 2004 Jun;12(6):1057-65. PMID:15274925
Page seeded by OCA on Sun Mar 30 23:29:44 2008
