1n0y

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(New page: 200px<br /><applet load="1n0y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n0y, resolution 1.75&Aring;" /> '''Crystal Structure of...)
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[[Image:1n0y.jpg|left|200px]]<br /><applet load="1n0y" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1n0y, resolution 1.75&Aring;" />
 
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'''Crystal Structure of Pb-bound Calmodulin'''<br />
 
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==Overview==
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==Crystal Structure of Pb-bound Calmodulin==
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Calmodulin (CaM) regulates a variety of cellular processes by interacting, with a large number of proteins in a Ca(2+)-dependent manner., Conformational flexibility plays a key role in CaM function, although the, full extent and detailed features of this flexibility are not fully, characterized. Here, the 1.75 A resolution crystal structure of, Pb(2+)-bound Paramecium tetraurelia CaM crystallized in a previously, unobserved monoclinic lattice is reported. Pb(2+)-CaM is disordered in, this new lattice and only a portion of each of the two molecules in the, asymmetric unit can be modeled. Comparison of the structures of Ca(2+)-CaM, and Pb(2+)-CaM show close agreement in the C-terminal domain but, significant structural differences in the N-terminal domain. In addition, translation-libration-screw (TLS) refinement and Rosenfield difference, analysis reveal inter-helical flexibility in the metal-bound N-terminal, domain of the protein that is absent in the metal-bound C-terminal domain, and indicates that the two structurally similar domains of CaM are, dynamically distinct. These results demonstrate that TLS refinement and, Rosenfield difference analysis allow detailed information about, macromolecular flexibility to be extracted from X-ray diffraction data, even when the crystal lattice prohibits full manifestation of this, flexibility.
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<StructureSection load='1n0y' size='340' side='right'caption='[[1n0y]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1n0y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N0Y FirstGlance]. <br>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n0y OCA], [https://pdbe.org/1n0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n0y RCSB], [https://www.ebi.ac.uk/pdbsum/1n0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n0y ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CALM_PARTE CALM_PARTE] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n0/1n0y_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1n0y ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1N0Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia] with PB, CAC and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N0Y OCA].
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Domain flexibility in the 1.75 A resolution structure of Pb2+-calmodulin., Wilson MA, Brunger AT, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1782-92. Epub 2003, Sep 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14501118 14501118]
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[[Category: Large Structures]]
[[Category: Paramecium tetraurelia]]
[[Category: Paramecium tetraurelia]]
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[[Category: Single protein]]
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[[Category: Brunger AT]]
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[[Category: Brunger, A.T.]]
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[[Category: Wilson MA]]
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[[Category: Wilson, M.A.]]
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[[Category: ACT]]
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[[Category: CAC]]
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[[Category: PB]]
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[[Category: calmodulin]]
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[[Category: lead]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:51:39 2007''
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Current revision

Crystal Structure of Pb-bound Calmodulin

PDB ID 1n0y

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