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1c1g

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(New page: 200px<br /><applet load="1c1g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c1g, resolution 7.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1c1g.gif|left|200px]]<br /><applet load="1c1g" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1c1g, resolution 7.0&Aring;" />
 
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'''CRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM==
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Tropomyosin is a 400A-long coiled coil that polymerizes to form a, continuous filament that associates with actin in muscle and numerous, non-muscle cells. Tropomyosin and troponin together form a, calcium-sensitive switch that is responsible for thin-filament regulation, of striated muscle. Subtle structural features of the molecule, including, non-canonical aspects of its coiled-coil motif, undoubtedly influence its, association with f-actin and its role in thin filament regulation., Previously, careful inspection of native diffraction intensities was, sufficient to construct a model of tropomyosin at 9A resolution in a, spermine-induced crystal form that diffracts anisotropically to 4A, resolution. Single isomorphous replacement (SIR) phasing has now provided, an empirical determination of the structure at 7A resolution. A novel, method of heavy-atom analysis was used to overcome difficulties in, interpretation of extremely anisotropic diffraction. The packing, arrangement of the molecules in the crystal, and important aspects of the, tropomyosin geometry such as non-uniformities of the pitch and variable, bending and radius of the coiled coil are evident.
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<StructureSection load='1c1g' size='340' side='right'caption='[[1c1g]], [[Resolution|resolution]] 7.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1c1g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C1G 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]] 7&#8491;</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=1c1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c1g OCA], [https://pdbe.org/1c1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c1g RCSB], [https://www.ebi.ac.uk/pdbsum/1c1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c1g ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPM1_PIG TPM1_PIG] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
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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/c1/1c1g_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=1c1g 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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1C1G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C1G OCA].
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*[[Tropomyosin|Tropomyosin]]
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*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
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==Reference==
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__TOC__
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Crystal structure of tropomyosin at 7 Angstroms resolution., Whitby FG, Phillips GN Jr, Proteins. 2000 Jan 1;38(1):49-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10651038 10651038]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Jr., G.N.Phillips.]]
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[[Category: Phillips Jr GN]]
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[[Category: Whitby, F.G.]]
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[[Category: Whitby FG]]
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[[Category: tropomyosin coiled-coil alpha-helical]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:04:37 2007''
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Current revision

CRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM

PDB ID 1c1g

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