1wpg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1wpg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wpg, resolution 2.30&Aring;" /> '''Crystal structure of...)
Current revision (07:42, 23 October 2024) (edit) (undo)
 
(19 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1wpg.jpg|left|200px]]<br /><applet load="1wpg" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1wpg, resolution 2.30&Aring;" />
 
-
'''Crystal structure of the SR CA2+-ATPase with MGF4'''<br />
 
-
==Overview==
+
==Crystal structure of the SR CA2+-ATPase with MGF4==
-
P-type ion transporting ATPases are ATP-powered ion pumps that establish, ion concentration gradients across biological membranes. Transfer of bound, cations to the lumenal or extracellular side occurs while the ATPase is, phosphorylated. Here we report at 2.3 A resolution the structure of the, calcium-ATPase of skeletal muscle sarcoplasmic reticulum, a representative, P-type ATPase that is crystallized in the absence of Ca2+ but in the, presence of magnesium fluoride, a stable phosphate analogue. This and, other crystal structures determined previously provide atomic models for, all four principal states in the reaction cycle. These structures show, that the three cytoplasmic domains rearrange to move six out of ten, transmembrane helices, thereby changing the affinity of the Ca2+-binding, sites and the gating of the ion pathway. Release of ADP triggers the, opening of the lumenal gate and release of phosphate its closure, effected, mainly through movement of the A-domain, the actuator of transmembrane, gates.
+
<StructureSection load='1wpg' size='340' side='right'caption='[[1wpg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1wpg]] is a 4 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=1WPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WPG 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]] 2.3&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MF4:TETRAFLUOROMAGNESATE(2-)'>MF4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TG1:(3S,3aR,4S,6S,6aR,7S,8S,9bS)-6-(acetyloxy)-4-(butanoyloxy)-3,3a-dihydroxy-3,6,9-trimethyl-8-{[(2Z)-2-methylbut-2-enoyl]oxy}-2-oxo-2,3,3a,4,5,6,6a,7,8,9b-decahydroazuleno[4,5-b]furan-7-yl+octanoate'>TG1</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=1wpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wpg OCA], [https://pdbe.org/1wpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wpg RCSB], [https://www.ebi.ac.uk/pdbsum/1wpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wpg ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/AT2A1_RABIT AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (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/wp/1wpg_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1wpg ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
P-type ion transporting ATPases are ATP-powered ion pumps that establish ion concentration gradients across biological membranes. Transfer of bound cations to the lumenal or extracellular side occurs while the ATPase is phosphorylated. Here we report at 2.3 A resolution the structure of the calcium-ATPase of skeletal muscle sarcoplasmic reticulum, a representative P-type ATPase that is crystallized in the absence of Ca2+ but in the presence of magnesium fluoride, a stable phosphate analogue. This and other crystal structures determined previously provide atomic models for all four principal states in the reaction cycle. These structures show that the three cytoplasmic domains rearrange to move six out of ten transmembrane helices, thereby changing the affinity of the Ca2+-binding sites and the gating of the ion pathway. Release of ADP triggers the opening of the lumenal gate and release of phosphate its closure, effected mainly through movement of the A-domain, the actuator of transmembrane gates.
-
==About this Structure==
+
Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues.,Toyoshima C, Nomura H, Tsuda T Nature. 2004 Nov 18;432(7015):361-8. Epub 2004 Sep 26. PMID:15448704<ref>PMID:15448704</ref>
-
1WPG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with MG, NA, MF4, ADP and TG1 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WPG OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues., Toyoshima C, Nomura H, Tsuda T, Nature. 2004 Nov 18;432(7015):361-8. Epub 2004 Sep 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15448704 15448704]
+
</div>
-
[[Category: Calcium-transporting ATPase]]
+
<div class="pdbe-citations 1wpg" style="background-color:#fffaf0;"></div>
-
[[Category: Oryctolagus cuniculus]]
+
-
[[Category: Single protein]]
+
-
[[Category: Nomura, H.]]
+
-
[[Category: Toyoshima, C.]]
+
-
[[Category: Tsuda, T.]]
+
-
[[Category: ADP]]
+
-
[[Category: MF4]]
+
-
[[Category: MG]]
+
-
[[Category: NA]]
+
-
[[Category: TG1]]
+
-
[[Category: had fold]]
+
-
[[Category: membrane protein]]
+
-
[[Category: p-type atpase]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:34:53 2007''
+
==See Also==
 +
*[[ATPase 3D structures|ATPase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Oryctolagus cuniculus]]
 +
[[Category: Nomura H]]
 +
[[Category: Toyoshima C]]
 +
[[Category: Tsuda T]]

Current revision

Crystal structure of the SR CA2+-ATPase with MGF4

PDB ID 1wpg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wpg"
Personal tools