1x02

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[[Image:1x02.gif|left|200px]]
 
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{{Structure
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==Solution structure of stereo array isotope labeled (SAIL) calmodulin==
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|PDB= 1x02 |SIZE=350|CAPTION= <scene name='initialview01'>1x02</scene>
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<StructureSection load='1x02' size='340' side='right'caption='[[1x02]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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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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|ACTIVITY=
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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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|GENE=
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x02 OCA], [http://www.ebi.ac.uk/pdbsum/1x02 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x02 RCSB]</span>
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== Function ==
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}}
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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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<div class="pdbe-citations 1x02" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1X02 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X02 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16511487 16511487]
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[[Category: Single protein]]
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[[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: sail]]
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[[Category: stereo array isotope labeling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:43:09 2008''
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Current revision

Solution structure of stereo array isotope labeled (SAIL) calmodulin

PDB ID 1x02

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