1rec: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1rec.gif|left|200px]]<br /><applet load="1rec" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rec, resolution 1.9&Aring;" />
'''THREE-DIMENSIONAL STRUCTURE OF RECOVERIN, A CALCIUM SENSOR IN VISION'''<br />


==Overview==
==THREE-DIMENSIONAL STRUCTURE OF RECOVERIN, A CALCIUM SENSOR IN VISION==
Recoverin, a recently discovered member of the EF hand superfamily, serves as a calcium sensor in vision. We report here the crystal structure of recombinant unmyristoylated recoverin at 1.9 A resolution. The four EF hands of the protein are arranged in a compact array that contrasts with the dumbbell shape of calmodulin and troponin C. A calcium ion is bound to EF hand 3, while EF hand 2 can bind samarium but not calcium in this crystal form. The other two EF hands have novel structural features that prevent or impair calcium binding. A concave hydrophobic surface formed by EF hands 1 and 2 may participate in the read out of calcium signals by recoverin and its homologs.
<StructureSection load='1rec' size='340' side='right'caption='[[1rec]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rec]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1REC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rec OCA], [https://pdbe.org/1rec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rec RCSB], [https://www.ebi.ac.uk/pdbsum/1rec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rec ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RECO_BOVIN RECO_BOVIN] Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.<ref>PMID:8097896</ref> <ref>PMID:8392055</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/1rec_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rec ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1REC 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=1REC OCA].
*[[Recoverin%2C a calcium-activated myristoyl switch|Recoverin%2C a calcium-activated myristoyl switch]]
 
== References ==
==Reference==
<references/>
Three-dimensional structure of recoverin, a calcium sensor in vision., Flaherty KM, Zozulya S, Stryer L, McKay DB, Cell. 1993 Nov 19;75(4):709-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8242744 8242744]
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Flaherty, K M.]]
[[Category: Flaherty KM]]
[[Category: Mckay, D B.]]
[[Category: Mckay DB]]
[[Category: Stryer, L.]]
[[Category: Stryer L]]
[[Category: Zozulya, S.]]
[[Category: Zozulya S]]
[[Category: CA]]
[[Category: calcium-binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:56 2008''

Latest revision as of 11:22, 14 February 2024

THREE-DIMENSIONAL STRUCTURE OF RECOVERIN, A CALCIUM SENSOR IN VISIONTHREE-DIMENSIONAL STRUCTURE OF RECOVERIN, A CALCIUM SENSOR IN VISION

Structural highlights

1rec is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RECO_BOVIN Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Hurley JB, Dizhoor AM, Ray S, Stryer L. Recoverin's role: conclusion withdrawn. Science. 1993 May 7;260(5109):740. PMID:8097896
  2. Kawamura S, Hisatomi O, Kayada S, Tokunaga F, Kuo CH. Recoverin has S-modulin activity in frog rods. J Biol Chem. 1993 Jul 15;268(20):14579-82. PMID:8392055

1rec, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA