1x02

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[[Image:1x02.png|left|200px]]
 
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==Solution structure of stereo array isotope labeled (SAIL) calmodulin==
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The line below this paragraph, containing "STRUCTURE_1x02", creates the "Structure Box" on the page.
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<StructureSection load='1x02' size='340' side='right'caption='[[1x02]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1x02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X02 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_1x02| PDB=1x02 | SCENE= }}
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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=1x02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x02 OCA], [https://pdbe.org/1x02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x02 RCSB], [https://www.ebi.ac.uk/pdbsum/1x02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x02 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] 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/x0/1x02_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=1x02 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Nuclear-magnetic-resonance spectroscopy can determine the three-dimensional structure of proteins in solution. However, its potential has been limited by the difficulty of interpreting NMR spectra in the presence of broadened and overlapping resonance lines and low signal-to-noise ratios. Here we present stereo-array isotope labelling (SAIL), a technique that can overcome many of these problems by applying a complete stereospecific and regiospecific pattern of stable isotopes that is optimal with regard to the quality and information content of the resulting NMR spectra. SAIL uses exclusively chemically and enzymatically synthesized amino acids for cell-free protein expression. We demonstrate for the 17-kDa protein calmodulin and the 41-kDa maltodextrin-binding protein that SAIL offers sharpened lines, spectral simplification without loss of information, and the ability to rapidly collect the structural restraints required to solve a high-quality solution structure for proteins twice as large as commonly solved by NMR. It thus makes a large class of proteins newly accessible to detailed solution structure determination.
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===Solution structure of stereo array isotope labeled (SAIL) calmodulin===
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Optimal isotope labelling for NMR protein structure determinations.,Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, Guntert P Nature. 2006 Mar 2;440(7080):52-7. PMID:16511487<ref>PMID:16511487</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16511487}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1x02" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16511487 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16511487}}
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==About this Structure==
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[[1x02]] is a 1 chain structure of [[Calmodulin]] with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X02 OCA].
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==See Also==
==See Also==
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*[[Calmodulin]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:16511487</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Guntert, P.]]
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[[Category: Guntert P]]
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[[Category: Kainosho, M.]]
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[[Category: Kainosho M]]
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[[Category: Ono, A M.]]
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[[Category: Ono AM]]
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[[Category: Terauchi, T.]]
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[[Category: Terauchi T]]
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[[Category: Torizawa, T.]]
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[[Category: Torizawa T]]
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[[Category: Metal binding protein]]
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[[Category: Sail]]
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[[Category: Stereo array isotope labeling]]
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Current revision

Solution structure of stereo array isotope labeled (SAIL) calmodulin

PDB ID 1x02

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