This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1a8y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:28, 7 February 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1a8y.gif|left|200px]]
 
-
{{Structure
+
==CRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTION==
-
|PDB= 1a8y |SIZE=350|CAPTION= <scene name='initialview01'>1a8y</scene>, resolution 2.4&Aring;
+
<StructureSection load='1a8y' size='340' side='right'caption='[[1a8y]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<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>
-
|ACTIVITY=
+
</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>
-
|GENE=
+
<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>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8y OCA], [http://www.ebi.ac.uk/pdbsum/1a8y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a8y RCSB]</span>
+
[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]]
-
'''CRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTION'''
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
 
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a8y_consurf.spt"</scriptWhenChecked>
-
==Overview==
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
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.
+
<text>to colour the structure by Evolutionary Conservation</text>
-
 
+
</jmolCheckbox>
-
==About this Structure==
+
</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].
-
1A8Y is a [[Single protein]] structure of sequence from [http://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].
+
<div style="clear:both"></div>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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://www.ncbi.nlm.nih.gov/pubmed/9628486 9628486]
+
[[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://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:35:47 2008''
+

Current revision

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

PDB ID 1a8y

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools