1rl3
From Proteopedia
(New page: 200px<br /><applet load="1rl3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rl3, resolution 2.70Å" /> '''Crystal structure of...) |
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| - | [[Image:1rl3.gif|left|200px]]<br /><applet load="1rl3" size=" | + | [[Image:1rl3.gif|left|200px]]<br /><applet load="1rl3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rl3, resolution 2.70Å" /> | caption="1rl3, resolution 2.70Å" /> | ||
'''Crystal structure of cAMP-free R1a subunit of PKA'''<br /> | '''Crystal structure of cAMP-free R1a subunit of PKA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In eukaryotes the primary target for cAMP, a ubiquitous second messenger, is cAMP-dependent protein kinase (PKA). Understanding how binding and | + | 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== | ==About this Structure== | ||
| - | 1RL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with PCG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=PCG:'>PCG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RL3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brown, S.]] | [[Category: Brown, S.]] | ||
| - | [[Category: Taylor, S | + | [[Category: Taylor, S S.]] |
[[Category: Wu, J.]] | [[Category: Wu, J.]] | ||
| - | [[Category: Xuong, N | + | [[Category: Xuong, N H.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: PCG]] | [[Category: PCG]] | ||
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[[Category: type 1a regulatory subunit]] | [[Category: type 1a regulatory subunit]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:01 2008'' |
Revision as of 12:52, 21 February 2008
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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 with and as ligands. 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 Thu Feb 21 14:52:01 2008
