2oa0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2oa0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oa0, resolution 3.400&Aring;" /> '''Crystal structure o...)
Current revision (10:33, 30 August 2023) (edit) (undo)
 
(19 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2oa0.gif|left|200px]]<br /><applet load="2oa0" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2oa0, resolution 3.400&Aring;" />
 
-
'''Crystal structure of Calcium ATPase with bound ADP and cyclopiazonic acid'''<br />
 
-
==Overview==
+
==Crystal structure of Calcium ATPase with bound ADP and cyclopiazonic acid==
-
The sarcoplasmic reticulum Ca(2+)-ATPase is essential for calcium reuptake, in the muscle contraction-relaxation cycle. Here we present structures of, a calcium-free state with bound cyclopiazonic acid (CPA) and magnesium, fluoride at 2.65 A resolution and a calcium-free state with bound CPA and, ADP at 3.4A resolution. In both structures, CPA occupies the calcium, access channel delimited by transmembrane segments M1-M4. Inhibition of, Ca(2+)-ATPase is stabilized by a polar pocket that surrounds the tetramic, acid of CPA and a hydrophobic platform that cradles the inhibitor. The, calcium pump residues involved include Gln(56), Leu(61), Val(62), and, Asn(101). We conclude that CPA inhibits the calcium pump by blocking the, calcium access channel and immobilizing a subset of transmembrane helices., In the E2(CPA) structure, ADP is bound in a distinct orientation within, the nucleotide binding pocket. The adenine ring is sandwiched between, Arg(489) of the nucleotide-binding domain and Arg(678) of the, phosphorylation domain. This mode of binding conforms to an adenine, recognition motif commonly found in ATP-dependent proteins.
+
<StructureSection load='2oa0' size='340' side='right'caption='[[2oa0]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2oa0]] 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=2OA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OA0 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]] 3.4&#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=CZA:(6AR,11AS,11BR)-10-ACETYL-9-HYDROXY-7,7-DIMETHYL-2,6,6A,7,11A,11B-HEXAHYDRO-11H-PYRROLO[1,2 2,3]ISOINDOLO[4,5,6-CD]INDOL-11-ONE'>CZA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2oa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oa0 OCA], [https://pdbe.org/2oa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oa0 RCSB], [https://www.ebi.ac.uk/pdbsum/2oa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oa0 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/oa/2oa0_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=2oa0 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The sarcoplasmic reticulum Ca(2+)-ATPase is essential for calcium reuptake in the muscle contraction-relaxation cycle. Here we present structures of a calcium-free state with bound cyclopiazonic acid (CPA) and magnesium fluoride at 2.65 A resolution and a calcium-free state with bound CPA and ADP at 3.4A resolution. In both structures, CPA occupies the calcium access channel delimited by transmembrane segments M1-M4. Inhibition of Ca(2+)-ATPase is stabilized by a polar pocket that surrounds the tetramic acid of CPA and a hydrophobic platform that cradles the inhibitor. The calcium pump residues involved include Gln(56), Leu(61), Val(62), and Asn(101). We conclude that CPA inhibits the calcium pump by blocking the calcium access channel and immobilizing a subset of transmembrane helices. In the E2(CPA) structure, ADP is bound in a distinct orientation within the nucleotide binding pocket. The adenine ring is sandwiched between Arg(489) of the nucleotide-binding domain and Arg(678) of the phosphorylation domain. This mode of binding conforms to an adenine recognition motif commonly found in ATP-dependent proteins.
-
==About this Structure==
+
The molecular basis for cyclopiazonic acid inhibition of the sarcoplasmic reticulum calcium pump.,Moncoq K, Trieber CA, Young HS J Biol Chem. 2007 Mar 30;282(13):9748-57. Epub 2007 Jan 26. PMID:17259168<ref>PMID:17259168</ref>
-
2OA0 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, CZA and ADP 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=2OA0 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
The molecular basis for cyclopiazonic acid inhibition of the sarcoplasmic reticulum calcium pump., Moncoq K, Trieber CA, Young HS, J Biol Chem. 2007 Mar 30;282(13):9748-57. Epub 2007 Jan 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17259168 17259168]
+
</div>
-
[[Category: Calcium-transporting ATPase]]
+
<div class="pdbe-citations 2oa0" style="background-color:#fffaf0;"></div>
-
[[Category: Oryctolagus cuniculus]]
+
-
[[Category: Single protein]]
+
-
[[Category: Moncoq, K.A.]]
+
-
[[Category: Young, H.S.]]
+
-
[[Category: ADP]]
+
-
[[Category: CZA]]
+
-
[[Category: MG]]
+
-
[[Category: calcium atpase]]
+
-
[[Category: cyclopiazonic acid]]
+
-
[[Category: mycotoxin]]
+
-
[[Category: serca]]
+
-
[[Category: x-ray crystallography]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:06:28 2007''
+
==See Also==
 +
*[[ATPase 3D structures|ATPase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Oryctolagus cuniculus]]
 +
[[Category: Moncoq KA]]
 +
[[Category: Young HS]]

Current revision

Crystal structure of Calcium ATPase with bound ADP and cyclopiazonic acid

PDB ID 2oa0

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/2oa0"
Personal tools