2het
From Proteopedia
(New page: 200px<br /><applet load="2het" size="450" color="white" frame="true" align="right" spinBox="true" caption="2het, resolution 3.0Å" /> '''Non-myristoylated bov...) |
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| - | [[Image:2het.gif|left|200px]]<br /><applet load="2het" size=" | + | [[Image:2het.gif|left|200px]]<br /><applet load="2het" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2het, resolution 3.0Å" /> | caption="2het, resolution 3.0Å" /> | ||
'''Non-myristoylated bovine recoverin (truncated at C-terminus) with calcium bound to EF-hand 3'''<br /> | '''Non-myristoylated bovine recoverin (truncated at C-terminus) with calcium bound to EF-hand 3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Recoverin is a Ca(2+)-regulated signal transduction modulator expressed in | + | Recoverin is a Ca(2+)-regulated signal transduction modulator expressed in the vertebrate retina that has been implicated in visual adaptation. An intriguing feature of recoverin is a cluster of charged residues at its C terminus, the functional significance of which is largely unclear. To elucidate the impact of this segment on recoverin structure and function, we have investigated a mutant lacking the C-terminal 12 amino acids. Whereas in myristoylated recoverin the truncation causes an overall decrease in Ca(2+) sensitivity, results for the non-myristoylated mutant indicate that the truncation primarily affects the high affinity EF-hand 3. The three-dimensional structure of the mutant has been determined by x-ray crystallography. In addition to significant changes in average coordinates compared with wild-type recoverin, the structure provides strong indication of increased conformational flexibility, particularly in the C-terminal domain. Based on these observations, we propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity. |
==About this Structure== | ==About this Structure== | ||
| - | 2HET 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 CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2HET 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=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HET OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Granzin, J.]] | [[Category: Granzin, J.]] | ||
| - | [[Category: Weiergraber, O | + | [[Category: Weiergraber, O H.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
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[[Category: recoverin]] | [[Category: recoverin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:07 2008'' |
Revision as of 15:41, 21 February 2008
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Non-myristoylated bovine recoverin (truncated at C-terminus) with calcium bound to EF-hand 3
Overview
Recoverin is a Ca(2+)-regulated signal transduction modulator expressed in the vertebrate retina that has been implicated in visual adaptation. An intriguing feature of recoverin is a cluster of charged residues at its C terminus, the functional significance of which is largely unclear. To elucidate the impact of this segment on recoverin structure and function, we have investigated a mutant lacking the C-terminal 12 amino acids. Whereas in myristoylated recoverin the truncation causes an overall decrease in Ca(2+) sensitivity, results for the non-myristoylated mutant indicate that the truncation primarily affects the high affinity EF-hand 3. The three-dimensional structure of the mutant has been determined by x-ray crystallography. In addition to significant changes in average coordinates compared with wild-type recoverin, the structure provides strong indication of increased conformational flexibility, particularly in the C-terminal domain. Based on these observations, we propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity.
About this Structure
2HET is a Single protein structure of sequence from Bos taurus with as ligand. Full crystallographic information is available from OCA.
Reference
Tuning of a neuronal calcium sensor., Weiergraber OH, Senin II, Zernii EY, Churumova VA, Kovaleva NA, Nazipova AA, Permyakov SE, Permyakov EA, Philippov PP, Granzin J, Koch KW, J Biol Chem. 2006 Dec 8;281(49):37594-602. Epub 2006 Oct 2. PMID:17015448
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