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New page: left|200px<br /> <applet load="2bl0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bl0, resolution 1.75Å" /> '''PHYSARUM POLYCEPHAL...
 
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[[Image:2bl0.gif|left|200px]]<br />
<applet load="2bl0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2bl0, resolution 1.75&Aring;" />
'''PHYSARUM POLYCEPHALUM MYOSIN II REGULATORY DOMAIN'''<br />


==Overview==
==Physarum polycephalum myosin II regulatory domain==
We have previously identified a single inhibitory Ca2+-binding site in the, first EF-hand of the essential light chain of Physarum conventional myosin, (Farkas, L., Malnasi-Csizmadia, A., Nakamura, A., Kohama, K., and Nyitray, L. (2003) J. Biol. Chem. 278, 27399-27405). As a general rule, conformation of the EF-hand-containing domains in the calmodulin family is, "closed" in the absence and "open" in the presence of bound cations; a, notable exception is the unusual Ca2+-bound closed domain in the essential, light chain of the Ca2+-activated scallop muscle myosin. Here we have, reported the 1.8 A resolution structure of the regulatory domain (RD) of, Physarum myosin II in which Ca2+ is bound to a canonical EF-hand that is, also in a closed state. The 12th position of the EF-hand loop, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16227209 (full description)]]
<StructureSection load='2bl0' size='340' side='right'caption='[[2bl0]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bl0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BL0 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]] 1.75&#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=2bl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bl0 OCA], [https://pdbe.org/2bl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bl0 RCSB], [https://www.ebi.ac.uk/pdbsum/2bl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bl0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9BJD3_PHYPO Q9BJD3_PHYPO]
== 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/bl/2bl0_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=2bl0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have previously identified a single inhibitory Ca2+-binding site in the first EF-hand of the essential light chain of Physarum conventional myosin (Farkas, L., Malnasi-Csizmadia, A., Nakamura, A., Kohama, K., and Nyitray, L. (2003) J. Biol. Chem. 278, 27399-27405). As a general rule, conformation of the EF-hand-containing domains in the calmodulin family is "closed" in the absence and "open" in the presence of bound cations; a notable exception is the unusual Ca2+-bound closed domain in the essential light chain of the Ca2+-activated scallop muscle myosin. Here we have reported the 1.8 A resolution structure of the regulatory domain (RD) of Physarum myosin II in which Ca2+ is bound to a canonical EF-hand that is also in a closed state. The 12th position of the EF-hand loop, which normally provides a bidentate ligand for Ca2+ in the open state, is too far in the structure to participate in coordination of the ion. The structure includes a second Ca2+ that only mediates crystal contacts. To reveal the mechanism behind the regulatory effect of Ca2+, we compared conformational flexibilities of the liganded and unliganded RD. Our working hypothesis, i.e. the modulatory effect of Ca2+ on conformational flexibility of RD, is in line with the observed suppression of hydrogen-deuterium exchange rate in the Ca2+-bound form, as well as with results of molecular dynamics calculations. Based on this evidence, we concluded that Ca2+-induced change in structural dynamics of RD is a major factor in Ca2+-mediated regulation of Physarum myosin II activity.


==About this Structure==
Structural evidence for non-canonical binding of Ca2+ to a canonical EF-hand of a conventional myosin.,Debreczeni JE, Farkas L, Harmat V, Hetenyi C, Hajdu I, Zavodszky P, Kohama K, Nyitray L J Biol Chem. 2005 Dec 16;280(50):41458-64. Epub 2005 Oct 13. PMID:16227209<ref>PMID:16227209</ref>
2BL0 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.32 3.6.1.32]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BL0 OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural evidence for non-canonical binding of Ca2+ to a canonical EF-hand of a conventional myosin., Debreczeni JE, Farkas L, Harmat V, Hetenyi C, Hajdu I, Zavodszky P, Kohama K, Nyitray L, J Biol Chem. 2005 Dec 16;280(50):41458-64. Epub 2005 Oct 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16227209 16227209]
</div>
<div class="pdbe-citations 2bl0" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Physarum polycephalum]]
[[Category: Physarum polycephalum]]
[[Category: Protein complex]]
[[Category: Debreczeni JE]]
[[Category: Debreczeni, J.E.]]
[[Category: Farkas L]]
[[Category: Farkas, L.]]
[[Category: Harmat V]]
[[Category: Harmat, V.]]
[[Category: Nyitray L]]
[[Category: Nyitray, L.]]
[[Category: CA]]
[[Category: ef-hand]]
[[Category: muscle protein]]
[[Category: myosin]]
[[Category: slime mould]]
 
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Retrieved from "https://proteopedia.org/2bl0"