2i94: Difference between revisions
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|PDB= 2i94 |SIZE=350|CAPTION= <scene name='initialview01'>2i94</scene> | |PDB= 2i94 |SIZE=350|CAPTION= <scene name='initialview01'>2i94</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Rhodopsin_kinase Rhodopsin kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.14 2.7.11.14] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Rhodopsin_kinase Rhodopsin kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.14 2.7.11.14] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i94 OCA], [http://www.ebi.ac.uk/pdbsum/2i94 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i94 RCSB]</span> | |||
}} | }} | ||
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[[Category: Rhodopsin kinase]] | [[Category: Rhodopsin kinase]] | ||
[[Category: Ames, J B.]] | [[Category: Ames, J B.]] | ||
[[Category: calcium]] | [[Category: calcium]] | ||
[[Category: ef-hand]] | [[Category: ef-hand]] | ||
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[[Category: recoverin]] | [[Category: recoverin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:41:10 2008'' | ||
Revision as of 03:41, 31 March 2008
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| Ligands: | |||||||
| Activity: | Rhodopsin kinase, with EC number 2.7.11.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR Structure of recoverin bound to rhodopsin kinase
OverviewOverview
Recoverin, a member of the neuronal calcium sensor branch of the EF-hand superfamily, serves as a calcium sensor that regulates rhodopsin kinase (RK) activity in retinal rod cells. We report here the NMR structure of Ca(2+)-bound recoverin bound to a functional N-terminal fragment of rhodopsin kinase (residues 1-25, called RK25). The overall main-chain structure of recoverin in the complex is similar to structures of Ca(2+)-bound recoverin in the absence of target (<1.8A root-mean-square deviation). The first eight residues of recoverin at the N terminus are solvent-exposed, enabling the N-terminal myristoyl group to interact with target membranes, and Ca(2+) is bound at the second and third EF-hands of the protein. RK25 in the complex forms an amphipathic helix (residues 4-16). The hydrophobic face of the RK25 helix (Val-9, Val-10, Ala-11, Ala-14, and Phe-15) interacts with an exposed hydrophobic groove on the surface of recoverin lined by side-chain atoms of Trp-31, Phe-35, Phe-49, Ile-52, Tyr-53, Phe-56, Phe-57, Tyr-86, and Leu-90. Residues of recoverin that contact RK25 are highly conserved, suggesting a similar target binding site structure in all neuronal calcium sensor proteins. Site-specific mutagenesis and deletion analysis confirm that the hydrophobic residues at the interface are necessary and sufficient for binding. The recoverin-RK25 complex exhibits Ca(2+)-induced binding to rhodopsin immobilized on concanavalin-A resin. We propose that Ca(2+)-bound recoverin is bound between rhodopsin and RK in a ternary complex on rod outer segment disk membranes, thereby blocking RK interaction with rhodopsin at high Ca(2+).
About this StructureAbout this Structure
2I94 is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for calcium-induced inhibition of rhodopsin kinase by recoverin., Ames JB, Levay K, Wingard JN, Lusin JD, Slepak VZ, J Biol Chem. 2006 Dec 1;281(48):37237-45. Epub 2006 Oct 4. PMID:17020884
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