1rl3
From Proteopedia
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|PDB= 1rl3 |SIZE=350|CAPTION= <scene name='initialview01'>1rl3</scene>, resolution 2.70Å | |PDB= 1rl3 |SIZE=350|CAPTION= <scene name='initialview01'>1rl3</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PRKAR1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |GENE= PRKAR1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1rgs|1RGS]], [[1ne4|1NE4]], [[1ne6|1NE6]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rl3 OCA], [http://www.ebi.ac.uk/pdbsum/1rl3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rl3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Wu, J.]] | [[Category: Wu, J.]] | ||
[[Category: Xuong, N H.]] | [[Category: Xuong, N H.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: PCG]] | ||
[[Category: camp-dependent protein kinase]] | [[Category: camp-dependent protein kinase]] | ||
[[Category: camp-free]] | [[Category: camp-free]] | ||
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[[Category: type 1a regulatory subunit]] | [[Category: type 1a regulatory subunit]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:29:44 2008'' |
Revision as of 20:29, 30 March 2008
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PRKAR1A (Bos taurus) | ||||||
| Related: | 1RGS, 1NE4, 1NE6
| ||||||
| 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
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