1a8y: Difference between revisions

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New page: left|200px<br /><applet load="1a8y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a8y, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1a8y.gif|left|200px]]<br /><applet load="1a8y" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1a8y, resolution 2.4&Aring;" />
'''CRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTION==
Calsequestrin, the major Ca2+ storage protein of muscle, coordinately, binds and releases 40-50 Ca2+ ions per molecule for each, contraction-relaxation cycle by an uncertain mechanism. We have determined, the structure of rabbit skeletal muscle calsequestrin. Three very negative, thioredoxin-like domains surround a hydrophilic center. Each monomer makes, two extensive dimerization contacts, both of which involve the approach of, many negative groups. This structure suggests a mechanism by which, calsequestrin may achieve high capacity Ca2+ binding. The suggested, mechanism involves Ca2+-induced collapse of the three domains and, polymerization of calsequestrin monomers arising from three factors:, N-terminal arm exchange, helix-helix contacts and Ca2+ cross bridges. This, proposed structure-based mechanism accounts for the observed coupling of, high capacity Ca2+ binding with protein precipitation.
<StructureSection load='1a8y' size='340' side='right'caption='[[1a8y]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1a8y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8Y FirstGlance]. <br>
1A8Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A8Y OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=1a8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8y OCA], [https://pdbe.org/1a8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8y RCSB], [https://www.ebi.ac.uk/pdbsum/1a8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8y ProSAT]</span></td></tr>
==Reference==
</table>
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum., Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH, Nat Struct Biol. 1998 Jun;5(6):476-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9628486 9628486]
== Function ==
[https://www.uniprot.org/uniprot/CASQ1_RABIT CASQ1_RABIT] Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. The release of calcium bound to calsequestrin through a calcium release channel triggers muscle contraction. The skeletal muscle isoform (CASQ1) binds around 80 Ca(2+) ions, while the cardiac isoform (CASQ2) binds approximately 60 Ca(2+) ions (By similarity).
== 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/a8/1a8y_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=1a8y ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Dunker AK]]
[[Category: Dunker, A.K.]]
[[Category: Kang C]]
[[Category: Kang, C.]]
[[Category: Liao H]]
[[Category: Liao, H.]]
[[Category: Trumble WR]]
[[Category: Trumble, W.R.]]
[[Category: Wang S]]
[[Category: Wang, S.]]
[[Category: Wesson CR]]
[[Category: Wesson, C.R.]]
[[Category: calcium-binding protein]]
[[Category: calsequestrin]]
[[Category: rabbit skeletal muscle]]
[[Category: sarcoplasmic reticulum]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:41:17 2007''

Latest revision as of 09:28, 7 February 2024

CRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTIONCRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTION

Structural highlights

1a8y is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CASQ1_RABIT Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. The release of calcium bound to calsequestrin through a calcium release channel triggers muscle contraction. The skeletal muscle isoform (CASQ1) binds around 80 Ca(2+) ions, while the cardiac isoform (CASQ2) binds approximately 60 Ca(2+) ions (By similarity).

Evolutionary Conservation

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

1a8y, resolution 2.40Å

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