1i84

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(New page: 200px<br /><applet load="1i84" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i84, resolution 20.0&Aring;" /> '''CRYO-EM STRUCTURE OF...)
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[[Image:1i84.gif|left|200px]]<br /><applet load="1i84" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1i84, resolution 20.0&Aring;" />
 
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'''CRYO-EM STRUCTURE OF THE HEAVY MEROMYOSIN SUBFRAGMENT OF CHICKEN GIZZARD SMOOTH MUSCLE MYOSIN WITH REGULATORY LIGHT CHAIN IN THE DEPHOSPHORYLATED STATE. ONLY C ALPHAS PROVIDED FOR REGULATORY LIGHT CHAIN. ONLY BACKBONE ATOMS PROVIDED FOR S2 FRAGMENT.'''<br />
 
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==Overview==
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==CRYO-EM STRUCTURE OF THE HEAVY MEROMYOSIN SUBFRAGMENT OF CHICKEN GIZZARD SMOOTH MUSCLE MYOSIN WITH REGULATORY LIGHT CHAIN IN THE DEPHOSPHORYLATED STATE. ONLY C ALPHAS PROVIDED FOR REGULATORY LIGHT CHAIN. ONLY BACKBONE ATOMS PROVIDED FOR S2 FRAGMENT.==
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Regulation of the actin-activated ATPase of smooth muscle myosin II is, known to involve an interaction between the two heads that is controlled, by phosphorylation of the regulatory light chain. However, the, three-dimensional structure of this inactivated form has been unknown. We, have used a lipid monolayer to obtain two-dimensional crystalline arrays, of the unphosphorylated inactive form of smooth muscle heavy meromyosin, suitable for structural studies by electron cryomicroscopy of unstained, frozen-hydrated specimens. The three-dimensional structure reveals an, asymmetric interaction between the two myosin heads. The ATPase activity, of one head is sterically "blocked" because part of its actin-binding, interface is positioned onto the converter domain of the second head., ATPase activity of the second head, which can bind actin, appears to be, inhibited through stabilization of converter domain movements needed to, release phosphate and achieve strong actin binding. When the subfragment 2, domain of heavy meromyosin is oriented as it would be in an actomyosin, filament lattice, the position of the heads is very different from that, needed to bind actin, suggesting an additional contribution to ATPase, inhibition in situ.
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<StructureSection load='1i84' size='340' side='right'caption='[[1i84]], [[Resolution|resolution]] 20.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1i84]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I84 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</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=1i84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i84 OCA], [https://pdbe.org/1i84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i84 RCSB], [https://www.ebi.ac.uk/pdbsum/1i84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i84 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYH11_CHICK MYH11_CHICK] Muscle contraction.
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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/i8/1i84_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=1i84 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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Regulation of the actin-activated ATPase of smooth muscle myosin II is known to involve an interaction between the two heads that is controlled by phosphorylation of the regulatory light chain. However, the three-dimensional structure of this inactivated form has been unknown. We have used a lipid monolayer to obtain two-dimensional crystalline arrays of the unphosphorylated inactive form of smooth muscle heavy meromyosin suitable for structural studies by electron cryomicroscopy of unstained, frozen-hydrated specimens. The three-dimensional structure reveals an asymmetric interaction between the two myosin heads. The ATPase activity of one head is sterically "blocked" because part of its actin-binding interface is positioned onto the converter domain of the second head. ATPase activity of the second head, which can bind actin, appears to be inhibited through stabilization of converter domain movements needed to release phosphate and achieve strong actin binding. When the subfragment 2 domain of heavy meromyosin is oriented as it would be in an actomyosin filament lattice, the position of the heads is very different from that needed to bind actin, suggesting an additional contribution to ATPase inhibition in situ.
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==About this Structure==
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Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2.,Wendt T, Taylor D, Trybus KM, Taylor K Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4361-6. Epub 2001 Apr 3. PMID:11287639<ref>PMID:11287639</ref>
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1I84 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Myosin_ATPase Myosin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.1 3.6.4.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I84 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2., Wendt T, Taylor D, Trybus KM, Taylor K, Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4361-6. Epub 2001 Apr 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11287639 11287639]
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</div>
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[[Category: Gallus gallus]]
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<div class="pdbe-citations 1i84" style="background-color:#fffaf0;"></div>
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[[Category: Myosin ATPase]]
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[[Category: Protein complex]]
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[[Category: Taylor, D.]]
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[[Category: Taylor, K.]]
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[[Category: Trybus, K.M.]]
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[[Category: Wendt, T.]]
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[[Category: coiled-coil]]
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[[Category: essential light chain]]
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[[Category: heavy meromyosin]]
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[[Category: motor protein]]
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[[Category: muscle protein]]
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[[Category: myosin subfragment 2]]
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[[Category: regulatory light chain]]
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[[Category: smooth muscle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:08:32 2007''
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==See Also==
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*[[Myosin 3D Structures|Myosin 3D Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gallus gallus]]
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[[Category: Large Structures]]
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[[Category: Taylor D]]
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[[Category: Taylor K]]
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[[Category: Trybus KM]]
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[[Category: Wendt T]]

Current revision

CRYO-EM STRUCTURE OF THE HEAVY MEROMYOSIN SUBFRAGMENT OF CHICKEN GIZZARD SMOOTH MUSCLE MYOSIN WITH REGULATORY LIGHT CHAIN IN THE DEPHOSPHORYLATED STATE. ONLY C ALPHAS PROVIDED FOR REGULATORY LIGHT CHAIN. ONLY BACKBONE ATOMS PROVIDED FOR S2 FRAGMENT.

PDB ID 1i84

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